protein Name methionineadenosyltransferase I, alpha caption image width HGNCid 6903 Symbol MAT1A AltSymbols EntrezGene 4143 OMIM 250850 RefSeq NM 000429 UniProt Q00266 PDB ECnumber Chromosome 10 Arm q Band 22 LocusSupplementaryData protein Name methionineadenosyltransferase II, alpha caption image width HGNCid 6904 Symbol MAT2A AltSymbols EntrezGene 4144 OMIM 601468 RefSeq NM 005911 UniProt P31153 PDB ECnumber Chromosome 2 Arm p Band 11.2 LocusSupplementaryData protein Name methionineadenosyltransferase II, beta caption image width HGNCid 6905 Symbol MAT2B AltSymbols EntrezGene 27430 OMIM 605527 RefSeq NM 013283 UniProt Q9NZL9 PDB ECnumber Chromosome 5 Arm q Band 34 LocusSupplementaryData q35 Methionineadenosyltransferase is an enzyme which catalyses the synthesis of S adenosylmethionine SAM from methionine and Adenosine triphosphate ATP . Conserved motifs in the 3 UTR of MAT2A mRNA A computational comparative analysis of vertebrate genome sequence s have identified a cluster of 6 conserved stem loop hairpin motifs in the 3 UTR of the MAT2A MRNA messenger RNA mRNA transcript. ref name pmid21994249 Cite pmid 21994249 ref The predicted hairpins named A F have strong evolutionary conservation and 3 of the predicted RNA structures hairpins A, C and D have been confirmed by Nucleic acid structure determination In line probing in line probing analysis. No structural changes were observed for any of the hairpins in the presence of metabolites SAM, S adenosylhomocysteine or L Methioninine. They are proposed to be involved in transcript stability and their functionality is currently under investigation. ref name pmid21994249 References reflist External links MeshName Methionineadenosyltransferase EC number 2.5.1.6 Alkyl and aryl transferases Amino acid metabolism enzymes biochemistry stub zh ... more details
SAM by 1 methionineadenosyltransferase . SAM serves as a methyl donor in many 2 methyltransferase ...chembox Verifiedfields changed verifiedrevid 462249884 Name Methionine ImageFile Methionin Methionine.svg ImageFile1 L methionine B 3D balls.png ImageSize1 220px ImageName1 Ball and stick model of the L isomer IUPACName Methionine OtherNames 2 amino 4 methylthio butanoic acid Section1 Chembox Identifiers ... EUIndex FlashPt Methionine IPAc en icon m a . n i n or IPAc en m a . n n abbreviated ... with cysteine , methionine is one of two sulfur containing proteinogenic amino acids. Its derivative S adenosyl methionine S adenosyl methionine SAM serves as a methyl donor. Methionine is an intermediate ... phospholipid s. Improper conversion of methionine can lead to atherosclerosis . ref Refsum ... used by plants for synthesis of ethylene . The process is known as the Shang Fa Yang Yang Cycle or the methionine cycle . Methionine is one of only two amino acids encoded by a single codon AUG in the standard ... mRNA. As a consequence, methionine is incorporated into the N terminal position of all protein s in eukaryote ... fed a diet without methionine developed steatohepatitis . Administration of methionine ameliorated the pathological consequences of methionine deprivation. ref Citation doi 10.1007 s10620 007 9900 7 author Oz HS, Chen TS, Neuman M title Methionine deficiency and hepatic injury in a dietary steatohepatitis ... 17710550 pmc 2271115 postscript . ref Zwitterions File Betain Methionin.png thumb none 400px S Methionine left and R methionine right in zwitterionic form at neutral pH Biosynthesis As an essential amino acid, methionine is not synthesized De novo synthesis de novo in humans, who must ingest methionine or methionine containing proteins. In plants and microorganisms, methionine is synthesized via a pathway ... methionine. Both cystathionine synthase and cystathionine lyase require Pyridoxal phosphate ... Vitamin B12 vitamin B sub 12 sub as a cofactor. ref Lehninger3rd . ref Enzymes involved in methionine ... more details
ja01131a519 ref It is made from adenosine triphosphate ATP and methionine by methionineadenosyltransferase ...DISPLAYTITLE S Adenosyl methionine chembox Verifiedfields changed verifiedrevid 476997975 Name S Adenosyl methionine ImageFile S Adenosyl methionine.png ImageSize 300px ImageFileR2 S adenosylmethionine.png ... butanoate OtherNames S Adenosyl L methionine ademetionine SAM e SAMe Section1 Chembox Identifiers ... methionine ademetionine , SAM , SAMe , SAM e is a common cosubstrate involved in methyl group transfers ... title The Nature of the Active Methyl Donor Formed Enzymatically from L Methionine and Adenosinetriphosphate ... group CH sub 3 sub attached to the methionine sulfur atom in SAM is chemically reactive. This allows ... riboswitch S box leader SAM riboswitch , which regulates genes involved in methionine or cysteine biosynthesis. Biochemistry of S adenosyl methionine SAM cycle The reactions that produce, consume ... EC 3.3.1.1 and the homocysteine recycled back to methionine through transfer of a methyl group from 5 methyltetrahydrofolate , by one of the two classes of methionine synthase s i.e. cobalamin dependent ... enzyme 2.1.1.14 EC 2.1.1.14 . This methionine can then be converted back to SAM, completing the cycle ... . ref cite journal author Roje S title S Adenosyl L methionine beyond the universal methyl group ... l methionine cite journal title The antidepressant potential of oral S adenosyl l methionine last ... http www.ncbi.nlm.nih.gov books bv.fcgi?rid hstat1a.chapter.2159 S Adenosyl L Methionine for Treatment ... M, Ortiz D, Chan A, Rogers E, Shea TB. title S adenosyl methionine A connection between nutritional ... from the amino acid L methionine through a metabolic pathway called the one carbon cycle, SAMe has ... title Role of S adenosyl L methionine in the treatment of depression a review of the evidence ... WI, Reinsch S, Hoehler F, Tobis JS, Harvey PW title S Adenosyl methionine SAMe versus celecoxib for the treatment ... methylation of DNA by the intracellular methyl group donor S adenosyl L methionine is a potentially ... more details
enzyme Name methionine S methyltransferase EC number 2.1.1.12 CAS number 9027 77 4 IUBMB EC number 2 1 1 12 GO code 0030732 image width caption In enzymology , a methionine S methyltransferase EC number 2.1.1.12 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine L methionine math rightleftharpoons math S adenosyl L homocysteine S methyl L methionine Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and L methionine , whereas its two product chemistry products are S adenosylhomocysteine and S methyl L methionine . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is S adenosyl L methionine L methionine S methyltransferase . Other names in common use include S adenosyl methioninemethionine methyl transferase , methionine methyltransferase , S adenosylmethionine transmethylase , and S adenosylmethionine methionine methyltransferase . This enzyme participates in selenoamino acid metabolism . It has 2 cofactor biochemistry cofactors manganese , and zinc . References reflist 1 cite journal author Karr D, Tweto J, Albersheim P date 1967 title S adenosyl methioninemethionine methyl transferase from wheat germ journal Arch. Biochem. Biophys. volume 121 pages 732&ndash 8 pmid 6078098 doi 10.1016 0003 9861 67 90061 6 issue 3 transferase stub Category EC 2.1.1 Category Manganese enzymes Category Zinc enzymes Category Enzymes of unknown structure it Metionina S metiltransferasi ja S ... more details
enzyme Name methionine racemase EC number 5.1.1.2 CAS number 9024 07 1 IUBMB EC number 5 1 1 2 GO code 0018111 image width caption In enzymology , a methionine racemase EC number 5.1.1.2 is an enzyme that catalysis catalyzes the chemical reaction L methionine math rightleftharpoons math D methionine Hence, this enzyme has one substrate biochemistry substrate , L methionine , and one product chemistry product , D methionine . This enzyme belongs to the family of isomerase s, specifically those racemase s and epimerase s acting on amino acid s and derivatives. The systematic name of this enzyme class is methionine racemase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 McElroy, W.D. and Glass, H.B. Eds. , A Symposium on Amino Acid Metabolism, A Symposium on Amino Acid Metabolism, Baltimore, 1955, p. 616 634. isomerase stub Category EC 5.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
Methionine oxidation is the Redox oxidation of the sulfur of the amino acid methionine resulting in methionine sulfoxide or methionine sulfone. The sulfur containing amino acids methionine and cysteine are more easily oxidized than the other amino acids. ref name BCLee Unlike oxidation of other amino acids, the oxidation of methionine can be reversed by enzymatic action, specifically by enzyme s in the methionine sulfoxide reductase family of enzymes. The three known methionine sulfoxide reductases are MSRA gene MsrA , MSRB2 MsrB , and fRmsr. ref name BCLee cite journal author Lee BC, Dikiy A, Kim HY, Gladyshev VN title Functions and evolution of selenoprotein methionine sulfoxide reductases ... pmc 3062201 doi 10.1016 j.bbagen.2009.04.014 ref Oxidation of methionine results in a mixture of the two diastereomer s methionine S sulfoxide and methionine R sulfoxide, which are reduced by MsrA and MsrB, respectively. ref cite journal author Kim HY, Gladyshev VN title Methionine sulfoxide reduction in mammals characterization of methionine R sulfoxide reductases journal MOLECULAR BIOLOGY OF THE CELL ... based methionine S sulfoxide, whereas MsrB is specific for protein based methionine R sulfoxide. fRmsr, however, catalyzes the reduction of free methionine R sulfoxide. ref name BCLee Thioredoxin serves to recycle by reduction some of the methionine sulfoxide reductase family of enzymes, whereas others ..., Kantorow M, Brot N, Weissbach H title Thionein can serve as a reducing agent for the methionine sulfoxide ... id pmid 16735467 doi 10.1073 pnas.0602826103 pmc 1592241 ref Methionine sulfoxide increases with age ... Remmen H, Richardson A, Wehr NB, Levine RL title Methionine oxidation and aging journal BIOCHEMICA ... doi 10.1016 S0891 5849 02 00824 9 ref Transgenic Drosophila fruit flies that overexpress methionine ... quality life extension by the enzyme peptide methionine sulfoxide reductase journal Proceedings of the National ... Card MetOx metox.htm Methionine oxidation chemistry Category Biochemistry Category Organic ... more details
enzyme Name methionine decarboxylase EC number 4.1.1.57 CAS number 37290 50 9 IUBMB EC number 4 1 1 57 GO code 0050095 image width caption In enzymology , a methionine decarboxylase EC number 4.1.1.57 is an enzyme that catalysis catalyzes the chemical reaction L methionine math rightleftharpoons math 3 methylthiopropanamine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L methionine , and two product chemistry products , 3 methylthiopropanamine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L methionine carboxy lyase 3 methylthiopropanamine forming . Other names in common use include L methionine decarboxylase , and L methionine carboxy lyase . References reflist 1 cite journal author Hagion H and Nakayama K date 1968 title Amino acid metabolism in microorganisms. Part IV. L Methionine decarboxylase produced by Streptomyces strain journal Agric. Biol. Chem. volume 32 pages 727&ndash 733 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
PBB geneid 4548 Methionine synthase also known as MS , MeSe , MetH is an enzyme that in humans is encoded ... LC, Banerjee R, Kruger WD title Cloning, mapping and RNA analysis of the human methionine synthase ... doi 10.1093 hmg 5.12.1851 url issn ref This enzyme is responsible for the regeneration of methionine from homocysteine . Methionine synthase forms part of the S adenosylmethionine SAMe biosynthesis ..., Matthews RG title Cobalamin dependent methionine synthase journal FASEB J. volume 4 issue 5 pages 1450 ... Function File Met pathway.gif thumb left Methionine synthase is enzyme 4 Methionine synthase catalyzes the final step in the regeneration of methionine from homocysteine . Methionine synthase contains ... cobalamin and releasing the product methionine . File VitaminB12 2.png thumb left The reaction reaction catalyzed by methionine synthase click to enlarge Clearleft Methionine synthase is the only mammalian enzyme that metabolizes 5 mTHF to regenerate the active cofactor THF. Deficiency in methionine ... B12 vitamin B sub 12 sub , or decreased levels of the enzyme methionine synthase reductase required for the sustained activity of methionine synthase . Clinical significance Mutations in the MTR gene ... G, or methylcobalamin deficiency cblG type . ref name entrez The consequence of reduced methionine synthase ... Cobalamin dependent methionine synthase. journal FASEB J. volume 4 issue 5 pages 1450 9 year 1990 pmid ... reductase and methionine synthase biochemistry and molecular biology. journal ... cite journal author Garovic Kocic V, Rosenblatt DS title Methionine auxotrophy in inborn errors of cobalamin ... analysis of the human methionine synthase gene. journal Hum. Mol. Genet. volume 5 issue 12 pages 1851 ..., et al. title Defects in human methionine synthase in cblG patients. journal Hum. Mol. Genet. volume ... D, Campeau E, Goyette P, et al. title Human methionine synthase cDNA cloning and identification of mutations ... journal author Chen LH, Liu ML, Hwang HY, et al. title Human methionine synthase. cDNA cloning, gene ... more details
enzyme Name cytochrome c methionine S methyltransferase EC number 2.1.1.123 CAS number 93585 98 9 IUBMB EC number 2 1 1 123 GO code 0030783 image width caption In enzymology , a cytochrome c methionine S methyltransferase EC number 2.1.1.123 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine cytochrome c methionine math rightleftharpoons math S adenosyl L homocysteine cytochrome c S methyl methionine Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and cytochrome c methionine , whereas its two product chemistry products are S adenosylhomocysteine and cytochrome c S methyl methionine . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is S adenosyl L methionine cytochrome c methionine S methyltransferase . References reflist 1 cite journal author Farooqui JZ, Tuck M, Paik WK year 1985 title Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochrome c journal J. Biol. Chem. volume 260 pages 537&ndash 45 pmid 2981218 issue 1 DEFAULTSORT Cytochrome C Methionine S Methyltransferase Category EC 2.1.1 Category Enzymes of unknown structure transferase stub it citocromo c metionina S metiltransferasi ... more details
enzyme Name methionine synthase reductase EC number 1.16.1.8 CAS number 207004 87 3 IUBMB EC number 1 16 1 8 GO code 0030586 image width caption In enzymology , a methionine synthase reductase EC number 1.16.1.8 is an enzyme that catalysis catalyzes the chemical reaction 2 methionine synthase methylcob I alamin 2 S adenosylhomocysteine NADP sup sup math rightleftharpoons math 2 methionine synthase cob I alamin NADPH H sup sup 2 S adenosyl L methionine The 3 substrate biochemistry substrates of this enzyme are methionine synthase methylcob I alamin , S adenosylhomocysteine , and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 4 product chemistry products are methionine synthase cob I alamin , nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and S adenosyl L methionine . This enzyme belongs to the family of oxidoreductase s, to be specific those oxidizing metal ion with NAD or NADP as acceptor. The systematic name of this enzyme class is methionine synthase methylcob I alamin,S adenosylhomocysteine NADP oxidoreductase . Other names in common use include methionine synthase cob II alamin reductase methylating , methionine synthase reductase , methionine synthase cobalamin methyltransferase cob II alamin , and reducing . It employs one cofactor biochemistry cofactor , flavoprotein . References reflist 1 cite journal author Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA date 1998 title Cloning and mapping of a cDNA for methionine ... cite journal author Olteanu H, Banerjee R date 2001 title Human methionine synthase reductase, a soluble P 450 reductase like dual flavoprotein, is sufficient for NADPH dependent methionine synthase ... of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase journal Biochemistry. volume 41 pages 13378&ndash 85 pmid 12416982 doi 10.1021 bi020536s issue 45 DEFAULTSORT Methionine synthase ... more details
enzyme Name D methionine pyruvate transaminase EC number 2.6.1.41 CAS number 37277 93 3 IUBMB EC number 2 6 1 41 GO code 0047306 image width caption In enzymology , a D methionine pyruvate transaminase EC number 2.6.1.41 is an enzyme that catalysis catalyzes the chemical reaction D methionine pyruvate math rightleftharpoons math 4 methylthio 2 oxobutanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are D methionine and pyruvate , whereas its two product chemistry products are 4 methylthio 2 oxobutanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is D methionine pyruvate aminotransferase . Other names in common use include D methionine transaminase , and D methionine aminotransferase . This enzyme participates in d alanine metabolism . References reflist 1 cite journal author Mapson LW, March JF, Wardale DA date 1969 title Biosynthesis of ethylene. 4 methylmercapto 2 oxobutyric acid an intermediate in the formation from methionine journal Biochem. J. volume 115 pages 653&ndash 61 pmid 5357015 issue 4 pmc 1185190 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name L methionine S S oxide reductase EC number 1.8.4.13 CAS number IUBMB EC number 1 8 4 13 GO code image width caption Orphan date February 2009 In enzymology , a L methionine S S oxide reductase EC number 1.8.4.13 is an enzyme that catalysis catalyzes the chemical reaction L methionine thioredoxin disulfide H sub 2 sub O math rightleftharpoons math L methionine S S oxide thioredoxin The 3 substrate biochemistry substrates of this enzyme are L methionine , thioredoxin disulfide , and water H sub 2 sub O , whereas its two product chemistry products are L methionine S S oxide and thioredoxin . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is L methionine thioredoxin disulfide S oxidoreductase . Other names in common use include fSMsr , methyl sulfoxide reductase I and II , acetylmethionine sulfoxide reductase , methionine sulfoxide reductase , L methionine oxidized thioredoxin S oxidoreductase , methionine S oxide reductase , and free methionine S S oxide reductase . This enzyme participates in methionine metabolism . References reflist 1 cite journal author Black S, Harte EM, Hudson B and Wartofsky L date 1960 title A specific enzymatic reduction of L methionine sulfoxide and a related nonspecific reduction of diulfides journal J. Biol. Chem. volume 235 pages 2910&ndash 2916 cite journal author Ejiri SI, Weissbach H, Brot N date 1979 title Reduction of methionine sulfoxide to methionine by Escherichia coli journal J. Bacteriol. volume 139 pages 161&ndash 4 pmid 37234 issue 1 pmc 216841 cite journal author Ejiri SI, Weissbach H, Brot N date 1980 title The purification of methionine sulfoxide reductase from Escherichia coli journal Anal. Biochem. volume 102 pages 393&ndash 8 pmid 6999943 doi 10.1016 0003 2697 80 90173 6 issue 2 cite journal author Weissbach H, Resnick L, Brot N date 2005 title Methionine sulfoxide reductases history ... more details
enzyme Name methionine gamma lyase EC number 4.4.1.11 CAS number 42616 25 1 IUBMB EC number 4 4 1 11 GO code 0018826 image width caption In enzymology , a methionine gamma lyase EC number 4.4.1.11 is an enzyme that catalysis catalyzes the chemical reaction L methionine H sub 2 sub O math rightleftharpoons math methanethiol NH sub 3 sub 2 oxobutanoate Thus, the two substrate biochemistry substrates of this enzyme are L methionine and water H sub 2 sub O , whereas its 3 product chemistry products are methanethiol , ammonia NH sub 3 sub , and 2 oxobutanoate . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is L methionine methanethiol lyase deaminating 2 oxobutanoate forming . Other names in common use include L methioninase , methionine lyase , methioninase , methionine dethiomethylase , L methionine gamma lyase , and L methionine methanethiol lyase deaminating . This enzyme participates in selenoamino acid metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1E5E , PDB link 1E5F , PDB link 1GC0 , PDB link 1GC2 , PDB link 1PFF , PDB link 1PG8 , PDB link 1UKJ , and PDB link 1Y4I . References reflist 1 cite journal author Kreis W, Hession C date 1973 title Isolation and purification of L methionine alpha deamino gamma mercaptomethane lyase L methioninase from Clostridium sporogenes journal Cancer. Res. volume 33 pages 1862&ndash 5 pmid 4720797 issue 8 enzyme stub Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name methionine glyoxylate transaminase EC number 2.6.1.73 CAS number 116155 75 0 IUBMB EC number 2 6 1 73 GO code 0050094 image width caption In enzymology , a methionine glyoxylate transaminase EC number 2.6.1.73 is an enzyme that catalysis catalyzes the chemical reaction L methionine glyoxylate math rightleftharpoons math 4 methylthio 2 oxobutanoate glycine Thus, the two substrate biochemistry substrates of this enzyme are L methionine and glyoxylate , whereas its two product chemistry products are 4 methylthio 2 oxobutanoate and glycine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L methionine glyoxylate aminotransferase . Other names in common use include methionine glyoxylate aminotransferase , and MGAT . References reflist 1 cite journal author BE date 1988 title Allylglucosinolate biosynthesis in Brassica carinata journal Phytochemistry journal Phytochemistry volume 27 pages 1345&ndash 1348 doi 10.1016 0031 9422 88 80190 0 last2 Chapple first2 Clint C.S. last3 Rothwell first3 Sue last4 Tober first4 Ingrid last5 Ellis first5 Brian E. Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
Mepron is the brand name for a time released, rumen protected Methionine DL Methionine capsule for dairy cattle. It is a registered trademark of Evonik Industries. Product The product is a 1.8 mm x 3 mm, nearly white cylindrical granule. The granules are free flowing, and nearly insoluble in water. The product is nearly dust free, and has a high level of durability. ref http www.makemilknotmanure.com technical.php ref It is coated in Ethyl cellulose ethylcellulose , a rugged and durable fiber. Mepron is also heat and pH tolerant, and has a long shelf life. ref http www.zayand.com Specifications.htm ref Uses Dairy herd milk production may be limited by the amino acid methionine therefore, the amino acid is included in cattle rations to provide a well balanced diet. ref Patton, R.A. Effect of rumen protected methionine on feed intake, milk production, true milk protein concentraition, and true milk protein yield, and the factors that influence these effects A meta analysis. Journal of Dairy Science, 93 2010 2105 2118. ref Normally a cow receives 10 20 grams of Mepron per day, depending on performance and ration composition. ref http www.makemilknotmanure.com technical.php ref According to a 2006 study, results suggest that RPM rumen protected methionine may be needed to improve milk production in Holstein cows with a mean production of 35 kg d small 1 small milk, fed with a diet based on alfalfa and corn silage. The optimum response was obtained with the addition of 16 g d small 1 small of ruminally protected methionine. Further studies are needed to determine if cows may respond to lysine supply once the methionine requirements are met. ref Lara, A. Milk production in Holstein cows supplemented with different levels of ruminally protected methionine. Livestock Science. 105. 2006 105 108. ref Safety Mepron can be handled safely and is non toxic, according ... Methionine http nutrients.umd.edu aa.htm Amino acids for dairy cattle http www.zayand.com Specifications.htm ... more details
enzyme Name methionine tRNA ligase EC number 6.1.1.10 CAS number 9033 22 1 IUBMB EC number 6 1 1 10 GO code 0004825 image width caption In enzymology , a methionine tRNA ligase EC number 6.1.1.10 is an enzyme that catalysis catalyzes the chemical reaction ATP L methionine tRNAMet math rightleftharpoons math AMP diphosphate L methionyl tRNAMet The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L methionine , and tRNA Met , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L methionyl tRNA Met . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L methionine tRNAMet ligase AMP forming . Other names in common use include methionyl tRNA synthetase , methionyl transfer ribonucleic acid synthetase , methionyl transfer ribonucleate synthetase , methionyl transfer RNA synthetase , methionine translase , and MetRS . This enzyme participates in 3 metabolism metabolic pathways methionine metabolism , selenoamino acid metabolism , and aminoacyl trna biosynthesis . Structural studies As of late 2007, 21 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1A8H , PDB link 1F4L , PDB link 1MEA , PDB link 1MED , PDB link 1MKH , PDB link 1P7P , PDB link 1PFU , PDB link 1PFV , PDB link 1PFW , PDB link 1PFY , PDB link 1PG0 , PDB link 1PG2 , PDB link 1QQT , PDB link 1RQG , PDB link 1WOY , PDB link 2CSX , PDB link 2CT8 , PDB link 2D54 , PDB link 2D5B , PDB link 2DJV , and PDB link 2HSN . References reflist 1 cite journal author Bergmann FH, Berg P and Dieckmann M date 1961 title The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The preparation of leucyl , valyl , isoleucyl and methionyl ribonucleic acid synthetases from Escherichia coli journal J. Biol. Chem. volume 236 pages 1735&ndash 1740 ... more details
OrganicBox complete wiki name Methionine name S 2 amino 4 methylsulfanyl butanoic acid GENERAL INFORMATION C 5 H 11 N 1 O 2 S 1 mass 149.21 abbreviation M, Met image Image L methionine skeletal.png 150px Image L methionine 3D sticks.png 140px synonyms ? DATABASES SMILES CSCCC C O O N InChI InChI 1 C5H11NO2S c1 9 3 2 4 6 5 7 8 h4H,2 3,6H2,1H3, H,7,8 f h7H L br 1 C5H11NO2S c1 9 3 2 4 6 5 7 8 h4H,2 3,6H2,1H3, H,7,8 t4 m0 s1 f h7H D CAS 63 68 3 DrugBank EINECS nowrap 200 562 9 ref 1 a PubChem nowrap 876 D ref 2 a , 6137 L ref 3 a PHYSICAL PROPERTIES Structure index of refraction abbe number dielectric constant magnetic susceptibility dipole moment U V data lambda max extinction coefficient Infrared data absorption bands NMR data proton NMR carbon NMR other NMR Spectrometry data mass spectrometry Phase behaviour delta fus H o delta fus S o delta vap H o delta vap S o triple point K triple point C triple point Pa criticle point K criticle point C criticle point Pa Solid properties delta f H o solid S o solid heat capacity solid density solid 1.340 melting point C 281 melting point F melting point K Liquid properties delta f H o liquid S o liquid heat capacity liquid density liquid viscosity liquid boiling point C boiling point F boiling point K Gas properties delta f H o gas S o gas heat capacity gas viscosity gas HAZARD PROPERTIES MSDS main hazards nfpa health nfpa flammability nfpa reactivity nfpa special flash point r phrases s phrases RTECS number CHEMICAL PROPERTIES XLogP 2.308 isoelectric point 5.74 disociation constant 2.16, 9.08 tautomers H bond donor 2 H bond acceptor 3 PHARMACOLOGICAL PROPERTIES References refbegin note 1 a EINECS 63 68 3 EINECS for L Methionine note 2 a PubChem 876 note 3 a PubChem 6137 refend AminoAcids Category Chemical data pages ar ... more details
Infobox protein family Symbol CobA CobO BtuR Name ATP corrinoid adenosyltransferase image PDB 1g5t EBI.jpg width caption the three dimensional structure of atp corrinoid adenosyltransferase from salmonella typhimurium. apo atp form Pfam PF02572 Pfam clan CL0023 InterPro IPR003724 SMART PROSITE MEROPS SCOP 1g64 TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol Cob adeno trans Name Cobalamin adenosyltransferase PduO EutT image PDB 1nog EBI.jpg width caption crystal structure of conserved protein 0546 from thermoplasma acidophilum Pfam PF01923 Pfam clan InterPro IPR002779 SMART PROSITE MEROPS SCOP 1nog TCDB OPM family OPM protein CAZy CDD In molecular biology, cob I yrinic acid a,c diamide adenosyltransferase also known as ATP cob I alamin or ATP corrinoid adenosyltransferase EC number 2.5.1.17 is an enzyme which catalyse s the conversion of cobalamin vitamin B12 into its coenzyme form, adenosylcobalamin coenzyme B12 . ref name pmid15516577 cite journal author Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR title Evidence that a B12 adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica journal J. Bacteriol. volume 186 issue 22 pages 7635 44 year 2004 month November pmid 15516577 pmc 524904 doi 10.1128 JB.186.22.7635 7644.2004 url ref Adenosylcobalamin AdoCbl is required for the ativity of certain enzyme s. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co C bond, and its synthesis is unique ... of the CobA type ATP Co I rrinoid adenosyltransferase enzyme of Methanosarcina mazei strain Go1 ... labile, metal containing ATP corrinoid adenosyltransferase enzyme journal J. Bacteriol. volume 186 ... of the Salmonella pduO gene, an ATP cob I alamin adenosyltransferase gene journal J. Bacteriol ... of cobA which encodes ATP corrinoid adenosyltransferase in Salmonella typhimurium journal Gene ... Purification and initial biochemical characterization of ATP Cob I alamin adenosyltransferase EutT ... more details
enzyme Name L methionine R S oxide reductase EC number 1.8.4.14 CAS number IUBMB EC number 1 8 4 14 GO code image width caption Orphan date February 2009 In enzymology , a L methionine R S oxide reductase EC number 1.8.4.14 is an enzyme that catalysis catalyzes the chemical reaction L methionine thioredoxin disulfide H sub 2 sub O math rightleftharpoons math L methionine R S oxide thioredoxin The 3 substrate biochemistry substrates of this enzyme are L methionine , thioredoxin disulfide , and water H sub 2 sub O , whereas its two product chemistry products are L methionine R S oxide and thioredoxin . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is L methionine thioredoxin disulfide S oxidoreductase L methionine R S oxide forming . Other names in common use include fRMsr , FRMsr , free met R o reductase , and free methionine R S oxide reductase . This enzyme participates in methionine metabolism . References reflist 1 cite journal author Etienne F, Spector D, Brot N, Weissbach H date 2003 title A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide journal Biochem. Biophys. Res. Commun. volume 300 pages 378&ndash 82 pmid 12504094 doi 10.1016 S0006 291X 02 02870 X issue 2 1.8 enzyme stub Category EC 1.8.4 Category Enzymes of unknown structure ja L R S ... more details
enzyme Name Peptide methionine R S oxide reductase EC number 1.8.4.12 CAS number IUBMB EC number 1 8 4 12 GO code image width caption Orphan date February 2009 In enzymology , a peptide methionine R S oxide ... L methionine thioredoxin disulfide H sub 2 sub O math rightleftharpoons math peptide L methionine R S oxide thioredoxin The 3 substrate biochemistry substrates of this enzyme are peptide L methionine ... L methionine R S oxide and thioredoxin . This enzyme belongs to the family of oxidoreductase ... name of this enzyme class is peptide methionine thioredoxin disulfide S oxidoreductase methionine R S oxide forming . Other names in common use include MsrB , methionine sulfoxide reductase ambiguous , pMSR , methionine S oxide reductase ambiguous , selenoprotein R , methionine S oxide reductase R form oxidizing , methionine sulfoxide reductase B , SelR , SelX , PilB , and pRMsr . References reflist 1 cite journal author Moskovitz J date 2002 title Purification and characterization of methionine ... S, Hart PJ date 2003 title Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein bound methionine journal J. Bacteriol. volume 185 pages 4119&ndash 26 pmid ... J date 2003 title Multiple methionine sulfoxide reductase genes in Staphylococcus aureus expression ... S, Olry A, Antoine M, Branlant G date 2005 title The enzymology and biochemistry of methionine sulfoxide ... doi 10.1016 j.bbapap.2004.09.016 cite journal author Ezraty B, Aussel L, Barras F date 2005 title Methionine ... L, Brot N date 2005 title Methionine sulfoxide reductases history and cellular role in protecting ... 2005 title The three dimensional structures of peptide methionine sulfoxide reductases current knowledge ... title Subcellular localization of methionine sulphoxide reductase A MsrA evidence for mitochondrial ... 2002 title Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence ... JF, Kantorow M, Brot N, Weissbach H date 2006 title Thionein can serve as a reducing agent for the methionine ... more details
Infobox Disease Name PAGENAME Image Methionin Methionine.svg Caption Methionine DiseasesDB 34424 ICD10 ICD10 E 72 1 e 70 ICD9 ICD9 270.4 ICDO OMIM MedlinePlus eMedicineSubj eMedicineTopic MeshID Hypermethioninemia is an excess of the amino acid methionine , in the blood. This condition can occur when methionine is not broken down properly in the body. Diagnosis People with hypermethioninemia often do not show any symptoms. Some individuals with hypermethioninemia exhibit learning disabilities, mental retardation , and other neurological problems delays in motor skills such as standing or walking sluggishness muscle weakness liver problems unusual facial features and their breath, sweat, or urine may have a smell resembling boiled cabbage. Hypermethioninemia can occur with other metabolic disorders, such as homocystinuria , tyrosinemia and galactosemia , which also involve the faulty breakdown of particular molecules. It can also result from liver disease or excessive dietary intake of methionine from consuming large amounts of protein or a methionine enriched infant formula. Pathophysiology Inherited hypermethioninemia that is not associated with other metabolic disorders can be caused by shortages in the enzymes that break down methionine. These enzymes are produced from the MAT1A , GNMT and AHCY genes. The reactions involved in metabolizing methionine help supply some of the amino acids needed for protein production. These reactions are also involved in transferring methyl groups, consisting of a carbon atom and three hydrogen atoms, from one molecule to another transmethylation , which is important in many cellular processes. The MAT1A gene provides instructions for producing the enzyme methionineadenosyltransferase . This enzyme converts methionine into a compound called ... homocysteine . Homocysteine may be converted back to methionine or into another amino acid, cysteine . A deficiency of any of these enzymes results in a buildup of methionine in the body, and may ... more details
enzyme Name Adenosyl fluoride synthase EC number 2.5.1.63 CAS number IUBMB EC number 2 5 1 63 GO code image width caption In enzymology , an adenosyl fluoride synthase EC number 2.5.1.63 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine fluoride math rightleftharpoons math 5 deoxy 5 fluoroadenosine L methionine Thus, the two substrate biochemistry substrates of this enzyme are S adenosyl L methionine and fluoride , whereas its two product chemistry products are 5 deoxy 5 fluoroadenosine and L methionine . This enzyme belongs to the family of transferase s, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S adenosyl L methionine fluoride adenosyltransferase . This enzyme is also called fluorinase . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1RQP , PDB link 1RQR , PDB link 2C2W , PDB link 2C4T , PDB link 2C4U , PDB link 2C5B , PDB link 2C5H , PDB link 2CBX , and PDB link 2CC2 . See also Carbon fluorine bond Organofluorine References reflist 1 cite journal author O Hagan D, Schaffrath C, Cobb SL, Hamilton JT, Murphy CD date 2002 title Biochemistry biosynthesis of an organofluorine molecule journal Nature. volume 416 pages 279 pmid 11907567 doi 10.1038 416279a issue 6878 cite journal author Naismith JH date 2004 title Crystal structure and mechanism of a bacterial fluorinating enzyme journal Nature. volume 427 pages 561&ndash 5 pmid 14765200 doi 10.1038 nature02280 last2 Huang first2 F last3 Deng first3 H last4 Schaffrath first4 C last5 Spencer first5 JB last6 O Hagan first6 D last7 Naismith first7 JH issue 6974 transferase stub Category EC 2.5.1 Category Enzymes of known structure ... more details
Infobox rfam Name SAM Chlorobi RNA image SAM Chlorobi RNA.svg width 450 caption Consensus secondary structure of SAM Chlorobi RNAs Symbol SAM Chlorobi RNA AltSymbols Rfam RF01724 miRBase miRBase family RNA type Cis regulatory element Tax domain Chlorobi GO SO CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData The SAM Chlorobi RNA motif is a conserved RNA structure that was identified by bioinformatics . ref name Weinberg2010 cite journal author Weinberg Z, Wang JX, Bogue J, et al. title Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea and their metagenomes journal Genome Biol volume 11 issue 3 pages R31 year 2010 month March pmid 20230605 doi 10.1186 gb 2010 11 3 r31 url pmc 2864571 ref The RNAs are found only in bacteria classified as within the phylum Chlorobi . These RNAs are always in the 5 untranslated region s of operon s that contain metK and ahcY genes. metK genes encode methionine adenosyltransferase , which synthesizes S adenosyl methionine SAM , and ahcY genes encode S adenosylhomocysteine hydrolase , which degrade the related metabolite S Adenosyl L homocysteine SAH . In fact all predicted metK and ahcY genes within Chlorobi bacteria as of 2010 are preceded by predicted SAM Chlorobi RNAs. ref name Weinberg2010 Predicted promoter biology promoter sequences are consistently found upstream of SAM Chlorobi RNAs, ref name Weinberg2010 and these promoter sequences imply that SAM Chlorobi RNAs are indeed transcription biology transcribed as RNAs. The promoter sequences are commonly associated with strong transcription in the phyla Chlorobi and Bacteroidetes , but are not used by most lineages of bacteria. The placement of SAM Chlorobi RNAs suggests that they are involved in the regulation of the metK ahcY operon through an unknown mechanism. References references External links Rfam id RF01724 name SAM Chlorobi RNA Category Cis regulatory RNA elements molecular cell biology stub ... more details
Cob I alamin adenosyltransferase and its interaction with methionine synthase reductase journal J. Biol ...PBB geneid 4552 Methionine synthase reductase, mitochondrial also known as MSR is an enzyme that in humans ... Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients ... sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 4552 accessdate ref Function Methionine ... is catalyzed by the enzyme methionine synthase . Methionine synthase eventually becomes inactive due to the oxidation of its cobalamin cob I alamin Cofactor biochemistry cofactor . Methionine synthase reductase regenerates a functional methionine synthase via reductive methylation. It is a member of the ferredoxin ... in homocystinuria are defective in reductive activation of methionine synthase. ref name entrez See also Methionine synthase References reflist External links http www.ncbi.nlm.nih.gov books NBK1328 ... refbegin 2 PBB Further reading citations cite journal author Wilson A title A common variant in methionine ... author Wilson A, Leclerc D, Rosenblatt DS, Gravel RA title Molecular basis for methionine synthase ... journal author Leclerc D title Molecular cloning, expression and physical mapping of the human methionine ... R title Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase journal ... author Zavadakova P title CblE type of homocystinuria due to methionine synthase reductase deficiency ... Multanowski M, Sanak M, Twardowska M title Polymorphisms of the 5,10 methylenetetrahydrofolate and the methionine ... MTHFR 677C T and methionine synthase reductase MTRR 66A G polymorphisms association with serum ... 6 issue 4 pages 371 82 year 2003 pmid 12810988 doi cite journal author Beyer K title Methionine ... cite journal author Bosco P title Methionine synthase MTR 2756 A G polymorphism, double heterozygosity methionine synthase 2756 AG methionine synthase reductase MTRR 66 AG, and elevated homocysteinemia ... more details
Infobox rfam Name SAM SAH riboswitch image SAM SAH riboswitch.svg width caption Consensus secondary structure of SAM SAH riboswitches Symbol SAM SAH riboswitch AltSymbols Rfam RF01727 miRBase miRBase family RNA type Riboswitch Tax domain Rhodobacterales GO SO CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData The SAM SAH riboswitch is a conserved RNA structure in certain bacteria that binds S Adenosyl methionine S adenosylmethionine SAM and S Adenosyl L homocysteine S adenosylhomocysteine SAH and is therefore presumed to be a riboswitch . ref name Weinberg2010 cite journal author Weinberg Z, Wang JX, Bogue J, et al. title Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea and their metagenomes journal Genome Biol volume 11 issue 3 pages R31 year 2010 month March pmid 20230605 doi 10.1186 gb 2010 11 3 r31 url pmc 2864571 ref SAM SAH riboswitches do not share any apparent structural resemblance to known riboswitches that bind SAM or SAH. The binding affinities for both compounds are similar, but binding for SAH is at least somewhat stronger. SAM SAH riboswitches are exclusively found in Rhodobacterales , an order biology order of alphaproteobacteria . They are always found in the apparent 5 untranslated region s of metK genes, which encode the enzyme Methionine adenosyltransferase that synthesizes SAM. Given this gene association, it was proposed that SAM SAH riboswitches more likely function as SAM sensing RNAs. SAM SAH riboswitches are relatively small among known riboswitches, which might relate to their inability to discriminate against SAH. However, the ability to reject SAH as a ligand might not be important under physiological conditions, because the cellular concentration of SAM is higher. ref cite journal author Ueland PM title Pharmacological and biochemical aspects of S adenosylhomocysteine and S adenosylhomocysteine hydrolase journal Pharmacol. Rev. volume 34 issue 3 pages 223 53 year 1982 ... more details
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