Protein Name PAGENAME image caption Symbol NAGS AltSymbols HGNCid 17996 Chromosome 17 Arm q Band 21.31 LocusSupplementaryData ECnumber 2.3.1.1 OMIM 608300 EntrezGene 162417 RefSeq NM 153006 UniProt Q8N159 PDB N acetylglutamate synthase is an enzyme that catalyses the production of N acetylglutamate from acetyl CoA and glutamate . This enzyme is important in bacteria and plants for the synthesis of arginine , an amino acid in the pathway. This enzyme is also important for mammals, because it produces the Urea cycle Regulation regulator of urea cycle N acetylglutamate, which activates carbamoyl phosphate synthetase I , which catalyses the initial reactions of urea cycle. Clinical significance Mutations in the gene are associated with N Acetylglutamate synthase deficiency . transferase stub References Lehninger principles of biochemistry, 4th edition, David L. Nelson, Michael M. Cox External links http www.ncbi.nlm.nih.gov books NBK1217 GeneReviews NCBI NIH UW entry on Urea Cycle Disorders Overview MeshName N Acetylglutamate Synthase Acyltransferases Urea cycle enzymes Mitochondrial enzymes Category Urea cycle fr N ac tylglutamate synthase it Amminoacido N acetiltransferasi zh N ... more details
refimprove date January 2008 Infobox Disease Name NAcetylglutamatesynthase deficiency Image N AcetylglutamicAcid.png Caption N Acetylglutamic acid Width 190px DiseasesDB 29823 ICD10 ICD9 ICDO OMIM 237310 MedlinePlus eMedicineSubj ped eMedicineTopic 10 MeshID NAcetylglutamatesynthase deficiency is an autosomal recessive urea cycle disorder . Mechanism Carbamoyl phosphate synthase I is an enzyme found in mitochondrial matrix and it catalyzes the very first reaction of the Urea cycle , in which carbamoyl phosphate is produced. Carbamoyl Phosphate Synthase 1, abbreviated as CPS1, is activated by its natural activator N Acetyl glutamate , which in turn is synthesized from acetyl CoA and glutamic acid in the reaction catalyzed by N Acetyl glutamate synthase , commonly called NAGS. N Acetyl Glutamate is required for the Urea cycle to take place. Deficiency in N Acetyl Glutamate Synthase or a genetic mutation in the gene coding for the enzyme, will lead to urea cycle failure in which ammonia is not converted to urea , but rather accumulated in blood leading to the condition called Type I Hyperammonemia . This is a severe neonatal disorder with fatal consequences, if not detected immediately upon birth. Genetics Image autorecessive.svg thumb right NAcetylglutamatesynthase deficiency has an autosomal recessive pattern of inheritance. The chromosome found to be carrying the gene encoding for N Acetyl Glutamate synthetase is chromosome 17 q q stands for longer arm of the chromosome in humans and chromosome 11 in mice. In both organisms, the chromosome consists of seven exons and six introns and non coding sequence . Image Geneprod.gif 450px thumb The figure shows human chromosome 17q and the coding region that encodes the NAGS enzyme. It has seven exons and six introns. The exons ... M, Cheng S, Packman S, Tuchman M title Null mutations in the Nacetylglutamatesynthase gene associated ... includes injections of structurally similar compound, N Carbamoyl L glutamate , an analogue of N Acetyl ... more details
N acetyllactosamine synthase is a galactosyltransferase enzyme. It is a component of lactose synthase . It is classified under EC number 2.4.1.90 . See also N Acetylglucosamine External links MeshName N acetyllactosamine synthase Glycosyltransferases Category EC 2.4.1 biochem stub it N acetillattosammina sintasi sr N acetillaktozamin sintaza ... more details
enzyme Name N acetylneuraminate synthase EC number 2.5.1.56 CAS number 37290 66 7 IUBMB EC number 2 5 1 56 GO code 0050462 image width caption In enzymology , a N acetylneuraminate synthase EC number 2.5.1.56 is an enzyme that catalysis catalyzes the chemical reaction phosphoenolpyruvate N acetyl D mannosamine H sub 2 sub O math rightleftharpoons math phosphate N acetylneuraminate The 3 substrate biochemistry substrates of this enzyme are phosphoenolpyruvate , N acetyl D mannosamine , and water H sub 2 sub O , whereas its two product chemistry products are phosphate and N acetylneuraminate . 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 phosphoenolpyruvate N acetyl D mannosamine C 1 carboxyvinyl transferase phosphate hydrolysing, 2 carboxy 2 oxoethyl forming . Other names in common use include NANA condensing enzyme , N acetylneuraminate pyruvate lyase pyruvate phosphorylating , and NeuAc synthase . This enzyme participates in aminosugars metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1WVO . References reflist 1 cite journal author BLACKLOW RS, WARREN L date 1962 title Biosynthesis of sialic acids by Neisseria meningitidis journal J. Biol. Chem. volume 237 pages 3520&ndash 6 pmid 13971393 cite journal doi 10.1271 bbb.61.2046 author Komaki E, Ohta Y, Tsukada Y date 1997 title Purification and characterization of N acetylneuraminate synthase from Escherichia coli K1 M12 journal Biosci. Biotechnol. Biochem. volume 61 pages 2046&ndash 50 pmid 9438985 issue 12 transferase stub Category EC 2.5.1 Category Enzymes of known structure ... more details
enzyme Name N acylneuraminate 9 phosphate synthase EC number 2.5.1.57 CAS number 9031 58 7 IUBMB EC number 2 5 1 57 GO code 0047444 image width caption In enzymology , a N acylneuraminate 9 phosphate synthase EC number 2.5.1.57 is an enzyme that catalysis catalyzes the chemical reaction phosphoenolpyruvate N acyl D mannosamine 6 phosphate H sub 2 sub O math rightleftharpoons math N acylneuraminate 9 phosphate phosphate The 3 substrate biochemistry substrates of this enzyme are phosphoenolpyruvate , N acyl D mannosamine 6 phosphate , and water H sub 2 sub O , whereas its two product chemistry products are N acylneuraminate 9 phosphate and phosphate . 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 phosphoenolpyruvate N acyl D mannosamine 6 phosphate 1 2 carboxy 2 oxoethyl transferase . Other names in common use include N acetylneuraminate 9 phosphate lyase , N acetylneuraminate 9 phosphate sialic acid 9 phosphate synthase , N acetylneuraminate 9 phosphate synthetase , N acylneuraminate 9 phosphate pyruvate lyase , pyruvate phosphorylating , and sialic acid 9 phosphate synthetase . This enzyme participates in aminosugars metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1WVO . References reflist 1 cite journal author Roseman S, Jourdian GW, Watson D and Rood R date 1961 title Enzymatic synthesis of sialic acid 9 phosphates journal Proc. Natl. Acad. Sci. USA volume 47 issue 7 pages 958&ndash 961 doi 10.1073 pnas.47.7.958 cite journal author Watson DR, Jourdian GW, Roseman S date 1966 title The sialic acids. 8. Sialic ... cloning and expression of the mouse N acetylneuraminic acid 9 phosphate synthase which does not have deaminoneuraminic acid KDN 9 phosphate synthase activity journal Biochem. Biophys. Res. Commun ... more details
enzyme Name isopenicillin Nsynthase EC number 1.21.3.1 CAS number 78642 31 6 IUBMB EC number 1 21 3 ... NSynthase. Active site iron is visible at center in gray. From Protein Data Bank PDB http www.ebi.ac.uk thornton srv databases cgi bin pdbsum GetPage.pl?pdbcode 1bk0 1BK0 Isopenicillin Nsynthase ... Nsynthase genes structure, function, diversity and evolution journal Trends Biotechnol. volume 8 ... The active site s of most isopenicillin N synthases contain an iron ion . ref name pmid9194566 cite journal author Roach PL, Clifton IJ, Hensgens CM, Shibata N, Schofield CJ, Hajdu J, Baldwin JE title Structure of isopenicillin Nsynthase complexed with substrate and the mechanism of penicillin formation ... active site of isopenicillin Nsynthase genetic and sequence analysis of the endogenous ligands ... be assembled from its component amino acids by N 5 amino 5 carboxypentanoyl L cysteinyl D valine synthase ACV synthase . ref name pmid11091371 cite journal author Schenk WA title Isopenicillin NSynthase ... Nsynthase in the formation of beta lactam antibiotics Following the IPNS pathway, further enzymes are responsible for the epimerization of isopenicillin N to penicillin N, the derivitazation to other ... title Substrate specificity of isopenicillin Nsynthase journal J. Med. Chem. volume 35 pages 1897 ... CJ, Baldwin JE date 1995 title Crystal structure of isopenicillin Nsynthase is the first from a new ... the formation of isopenicillin N from small L small aminoadipoyl small L small cysteinyl small D small valine small LLD small ACV . N 5 S 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine O sub 2 sub math rightleftharpoons math isopenicillin N 2 H sub 2 sub O This reaction ... 42990 url issn ref This enzyme is also called isopenicillin N synthetase . Mechanism File ACTIVE SITE Isopenicillin N synthase.JPG right thumb Close up rendering of active site of isopenicillin Nsynthase, showing His270, His214, Asp216 top left to right, clockwise , and a water molecule coordinating ... more details
reinhardti. II Purification and properties of Nacetylglutamate 5 phosphotransferase, the allosteric ...No footnotes date March 2010 enzyme Name acetylglutamate kinase EC number 2.7.2.8 CAS number 9027 58 1 IUBMB EC number 2 7 2 8 GO code 0003991 image width caption In enzymology , an acetylglutamate kinase EC number 2.7.2.8 is an enzyme that catalysis catalyzes the chemical reaction ATP N acetyl L glutamate math rightleftharpoons math ADP N acetyl L glutamyl 5 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and N acetyl L glutamic acid glutamate , whereas its two product chemistry products are adenosine diphosphate ADP and N acetyl L glutamyl 5 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a carboxy group as acceptor. This enzyme participates in urea cycle and metabolism of amino groups. Nomenclature The systematic name of this enzyme class is ATP N acetyl L glutamate 5 phosphotransferase . Other names in common use include Nacetylglutamate 5 phosphotransferase, acetylglutamate phosphokinase, Nacetylglutamate phosphokinase, Nacetylglutamate kinase, and N acetylglutamic 5 phosphotransferase. 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 1GS5 , PDB link 1GSJ , PDB link 1OH9 , PDB link 1OHA , PDB link 1OHB , PDB link 2AP9 , PDB link 2BTY , PDB link 2BUF , and PDB link 2RD5 . References reflist 1 cite journal author Baich A, Vogel HJ date 1962 title N Acetyl gamma Ilutamokinase and N acetylglutamic gamma semialdehyde dehydrogenase repressible enzymes of arginine synthesis in Escherichia coli journal Biochem. Biophys. Res. Commun. volume 7 pages 491&ndash 6 pmid 13863980 doi 10.1016 0006 291X 62 90342 ... title N Acetyl gamma glutamokinase Escherichia coli journal Methods Enzymol. volume 17A pages 251 ... more details
Refimprove date August 2007 In biochemistry , a synthase is an enzyme that catalyse s a Biosynthesis synthesis process. Following the Enzyme Commission number EC number classification, they belong to the group of lyase s, with ligase s catalysing the reverse reaction. Note that, originally, biochemical nomenclature distinguished synthetases and synthases. Under the original definition, synthases do not use energy from nucleoside triphosphates such as ATP, GTP, CTP, TTP, and UTP , whereas synthetases do use nucleoside triphosphates. However, the Joint Commission on Biochemical Nomenclature JCBN dictates that synthase can be used with any enzyme that catalyzes synthesis whether or not it uses nucleoside triphosphates , whereas synthetase is to be used synonymously with ligase . ref http www.chem.qmul.ac.uk iubmb newsletter misc synthase.html ref Examples ATP synthase Citrate synthase Tryptophan synthase Pseudouridine synthase Fatty acid synthase Cellulose synthase UDP forming Cellulose synthase GDP forming References references Enzymes Category Lyases Enzyme stub de Synthasen fr Synthase lt Sintaz pl Syntazy sv Syntas zh ... more details
Lactose synthase is an enzyme that generates lactose from glucose and UDP galactose . It is classified under EC number 2.4.1.22 . It consists of N acetyllactosamine synthase and alpha lactalbumin . Alpha lactalbumin, which is expressed in response to prolactin , increases the affinity of N acetyllactosamine synthase for its substrate, causing increased production of lactose during lactation. External links MeshName Lactose synthase Glycosyltransferases Fructose and galactose metabolism Category EC 2.4.1 biochem stub it Lattosio sintasi ja ... more details
enzyme Name 3 propylmalate synthase EC number 2.3.3.12 CAS number 37290 62 3 IUBMB EC number 2 3 3 12 GO code 0050442 image width caption In enzymology , a 3 propylmalate synthase EC number 2.3.3.12 is an enzyme that catalysis catalyzes the chemical reaction pentanoyl CoA H sub 2 sub O glyoxylate math rightleftharpoons math 3 propylmalate CoA The 3 substrate biochemistry substrates of this enzyme are pentanoyl CoA , water H sub 2 sub O , and glyoxylate , whereas its two product chemistry products are 3 propylmalate and coenzyme A CoA . This enzyme belongs to the family of transferase s, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is pentanoyl CoA glyoxylate C pentanoyltransferase thioester hydrolysing, 1 carboxybutyl forming . Other names in common use include 3 n propyl malate synthase , 3 propylmalate glyoxylate lyase CoA pentanoylating , beta n propylmalate synthase , and n propylmalate synthase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author IMAI K, REEVES HC, AJL SJ date 1963 title N PROPYLMALATE SYNTHETASE journal J. Biol. Chem. volume 238 pages 3193&ndash 8 pmid 14085361 transferase stub Category EC 2.3.3 Category Enzymes of unknown structure it 3 propilmalato sintasi ... more details
Lumazine synthase LS or more specifically 6,7 dimethyl 8 ribityllumazine synthase is a protein enzyme also known as riboflavin synthase which catalysis catalyses the penultimate step in the Biosynthesis synthesis of riboflavin . This protein is found in bacteria , archaea , plants and fungi , with a number of different quaternary structure s. However each of these proteins is homology biology homologous , sharing a common tertiary structure subunit fold . Icosahedral 60 subunit assemblies are found in spinach , Bacillus subtilis , and Aquifex aeolicus while pentamer ic 5 subunit assemblies are found in Brucella abortus , Saccharomyces cerevisiae and certain fungi. References cite journal author Fornasari MS, Laplagne DA, Frankel N, Cauerhff AA, Goldbaum FA, Echave J title Sequence determinants of quaternary structure in lumazine synthase journal Mol. Biol. Evol. volume 21 issue 1 pages 97 107 year 2004 pmid 14523158 doi 10.1093 molbev msg244 url http mbe.oxfordjournals.org cgi content abstract 21 1 97 br Category Enzymes enzyme stub ... more details
enzyme Name EPSP Synthase 3 phosphoshikimate 1 carboxyvinyltransferase EC number 2.5.1.19 CAS number 9068 73 9 IUBMB EC number 2 5 1 19 GO code 0003866 image EPSP synthase.PNG width caption EPSP synthase liganded with shikimate. ref name pmid16225867 cite journal author Priestman MA, Healy ML, Funke ... enolpyruvylshikimate 3 phosphate synthase with shikimate journal FEBS Lett. volume 579 issue 25 pages ... EPSP synthase Name EPSP synthase 3 phosphoshikimate 1 carboxyvinyltransferase image EPSP synthase cartoon.PNG width caption Ribbon diagram of EPSP synthase Pfam PF00275 InterPro IPR001986 SMART Prosite PDOC00097 SCOP 1eps TCDB OPM family OPM protein PDB 5 enolpyruvylshikimate 3 phosphate EPSP synthase ... names in common use include div col colwidth 25em 5 enolpyruvylshikimate 3 phosphate synthase, 3 enolpyruvylshikimate 5 phosphate synthase, 3 enolpyruvylshikimic acid 5 phosphate synthetase, 5 enolpyruvylshikimate 3 phosphate synthase, 5 enolpyruvyl 3 phosphoshikimate synthase, 5 enolpyruvylshikimate 3 phosphate synthetase, 5 enolpyruvylshikimate 3 phosphoric acid synthase, enolpyruvylshikimate phosphate synthase, and 3 phosphoshikimate 1 carboxyvinyl transferase. Div col end Function The enzyme ... E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W title Interaction of the herbicide glyphosate with its target enzyme 5 enolpyruvylshikimate 3 phosphate synthase in atomic detail ... s diet. Structure EPSP synthase is a monomeric enzyme. It is composed of two domains, which are joined ... to clamp down around the substrate in the active site. Reaction EPSP synthase catalyzes the reaction ... EPSP . File EPSPreactionII.tif 600px File EPSP synthase 2.png 200px EPSP, the product of the reaction ... the shikimate pathway. It targets EPSP synthase, the enzyme that catalyzes the conversion of shikimate ... state that transforms the reactants into products in the reaction that is catalyzed by EPSP synthase. Hence glyphosate as a transition state analog binds more tightly to EPSP synthase than its ... more details
enzyme Name 4 amino 4 deoxychorismate synthase EC number 6.3.5.8 CAS number 132264 37 0 IUBMB EC number 6 3 5 8 GO code 0046820 image width caption In enzymology , an aminodeoxychorismate synthase EC number 6.3.5.8 is an enzyme that catalysis catalyzes the chemical reaction chorismate L glutamine math rightleftharpoons math 4 amino 4 deoxychorismate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are chorismate and L glutamine , whereas its two product chemistry products are 4 amino 4 deoxychorismate and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is chorismate L glutamine amido ligase . Other names in common use include ADC synthase , 4 amino 4 deoxychorismate synthase , and PabB . This enzyme participates in folate biosynthesis . References reflist 1 cite journal author Ye QZ, Liu J, Walsh CT date 1990 title p Aminobenzoate synthesis in Escherichia coli purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase journal Proc. Natl. Acad. Sci. U. S. A. volume 87 pages 9391&ndash 5 pmid 2251281 doi 10.1073 pnas.87.23.9391 issue 23 pmc 55171 cite journal author Viswanathan VK, Green JM, Nichols BP date 1995 title Kinetic characterization of 4 amino 4 deoxychorismate synthase from Escherichia coli journal J. Bacteriol. volume 177 pages 5918&ndash 23 pmid 7592344 issue 20 pmc 177419 ligase stub Category EC 6.3.5 Category Enzymes of unknown structure ... more details
enzyme Name S linalool synthase EC number 4.2.3.25 CAS number IUBMB EC number 4 2 3 25 GO code image width caption Orphan date February 2009 In enzymology , a S linalool synthase EC number 4.2.3.25 is an enzyme that catalysis catalyzes the chemical reaction geranyl diphosphate H sub 2 sub O math rightleftharpoons math 3S linalool diphosphate Thus, the two substrate biochemistry substrates of this enzyme are geranyl diphosphate and water H sub 2 sub O , whereas its two product chemistry products are 3S linalool and diphosphate . This enzyme belongs to the family of lyase s, specifically those carbon oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl diphosphate diphosphate lyase 3S linalool forming . Other names in common use include LIS , Lis , and 3S linalool synthase . References reflist 1 cite journal author Pichersky E, Lewinsohn E, Croteau R date 1995 title Purification and characterization of S linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri journal Arch. Biochem. Biophys. volume 316 pages 803&ndash 7 pmid 7864636 doi 10.1006 abbi.1995.1107 issue 2 cite journal author Luecker J date 2001 title Expression of Clarkia S linalool synthase in transgenic petunia plants results in the accumulation of S linalyl beta D glucopyranoside journal Plant. J. volume 27 pages 315&ndash 24 pmid 11532177 doi 10.1046 j.1365 313x.2001.01097.x last2 Bouwmeester first2 HJ last3 Schwab first3 W last4 Blaas first4 J last5 Van Der Plas first5 LH last6 Verhoeven first6 HA issue 4 cite journal author Dudareva N, Cseke L, Blanc VM, Pichersky E date 1996 title Evolution of floral scent in Clarkia novel patterns of S linalool synthase gene expression in the C. breweri flower journal Plant. Cell. volume 8 pages 1137&ndash 48 pmid 8768373 doi 10.1105 tpc.8.7.1137 issue 7 pmc 161191 4.2 enzyme stub Category EC 4.2.3 Category Enzymes of unknown structure ... more details
protein Name Citrate synthase caption image width HGNCid 2422 Symbol CS AltSymbols EntrezGene 1431 OMIM ... The enzyme citrate synthase E.C. 2.3.3.1 previously 4.1.3.7 exists in nearly all living cells ... Weigand, Georg, and Steven J. Remington 1986 . Citrate Synthase Structure, Control, and Mechanism ...?cookieSet 1 ref Citrate synthase is localized within eukaryotic cells in the mitochondrial ... cytoplasmic ribosomes , then transported into the mitochondrial matrix. Citrate synthase is commonly used as a quantitative enzyme marker for the presence of intact mitochondria . Citrate synthase catalysis ... J. Remington 1986 . Citrate Synthase Structure, Control, and Mechanism. Ann. rev. Biophys. Biophys ... Synthase open form .png thumb 200px left The Active Site of Citrate Synthase open form Image Citrate synthase Closed form.png thumb 200px left The Active Site of Citrate Synthase closed form Citrate synthase s 437 amino acid residues are organized into two main subunits, each consisting of 20 alpha helices. These alpha helices compose approximately 75 of citrate synthase s tertiary structure , while ... acids of citrate synthase s active site in its open state the substrate is absent . ref PDB ID 1CSC ... display the tertiary structure of citrate synthase in its opened and closed form. The enzyme changes ... Changes of Citrate Synthase. Eur J Biochem. 120, 155 160 http www.blackwell synergy.com doi pdf 10.1111 j.1432 1033.1981.tb05683.x ref Mechanism Citrate Synthase has three key amino acids in its active ... and Co. Pages 608 609. ref Image Citrate Synthase Mechanism Drew Beck revised OH.png thumb 800px none Mechanism for Citrate Synthase including residues involved This http bcs.whfreeman.com lehninger pages bcs main.asp?v category&s 00010&n 16000&i 16010.01&o 00510 00520 00530 00540 00550 00PRS ... synthase s mechanism from Lehninger s Principles of Biochemistry page. ref Lehninger 2005 . Principles ... of citrate synthase by acetyl CoA analogues has also been well documented and has been ... more details
Chalcone synthases CHS are a family of polyketide synthase enzyme s associated with the production of chalcones , a class of organic compound s found mainly in plants as natural defense mechanisms and as synthetic intermediates, for example in the production of pigment s. Although higher plant chalcone synthases have been extensively studied, little information is available on the enzymes from bryophytes primitive plants . Cloning of CHS from the moss Physcomitrella patens revealed an important transition from the chalcone synthases present in microorganisms to those present in higher plants. ref name clark cite journal author Jiang C, Schommer C, Kim S Y, Suh D Y title Cloning and Characterization of Chalcone Synthase from the moss Physcomitrella patens journal Phytochemistry journal Phytochemistry volume 67 issue 23 pages 2531 2540 year 2006 pmid 17083952 doi 10.1016 j.phytochem.2006.09.030 ref The chalcone synthase gene of Petunia plants is famous for being the first gene in which the phenomenon of RNA interference was observed researchers intending to upregulate the production of pigments in light pink or violet flowers introduced a transgene for chalcone synthase, expecting that both the native gene and the transgene would express the enzyme and result in a more deeply colored flower phenotype . Instead the transgenic plants had mottled white flowers, indicating that the introduction of the transgene had downregulated or silenced chalcone synthase expression. ref name Napoli ... Synthase Gene into Petunia Results in Reversible Co Suppression of Homologous Genes in trans journal ... transcriptional inhibition of the chalcone synthase gene expression via an increased rate of messenger RNA degradation. ref name Van Blokland 1994 cite journal author Van Blokland R, Van der Geest N, Mol JNM, Kooter JM title Transgene mediated suppression of chalcone synthase expression in Petunia hybrida ... 313X.1994.6060861.x issue 6 ref Naringenin chalcone synthase uses malonyl CoA and 4 coumaroyl CoA ... more details
enzyme Name mycocerosate synthase EC number 2.3.1.111 CAS number 95229 19 9 IUBMB EC number 2 3 1 111 GO code 0050111 image width caption In enzymology , a mycocerosate synthase EC number 2.3.1.111 is an enzyme that catalysis catalyzes the chemical reaction acyl CoA n methylmalonyl CoA 2n NADPH 2n H sup sup math rightleftharpoons math multi methyl branched acyl CoA n CoA n CO sub 2 sub 2n NADP sup sup The 4 substrate biochemistry substrates of this enzyme are acyl CoA , methylmalonyl CoA , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup , whereas its 4 product chemistry products are multi methyl branched acyl CoA , coenzyme A CoA , carbon dioxide CO sub 2 sub , and nicotinamide adenine dinucleotide phosphate NADP sup sup . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl CoA methylmalonyl CoA C acyltransferase decarboxylating, oxoacyl and enoyl reducing . This enzyme is also called mycocerosic acid synthase . References reflist 1 cite journal author Rainwater DL, Kolattukudy PE date 1985 title Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n fatty acyl CoA with methylmalonyl CoA journal J. Biol. Chem. volume 260 pages 616&ndash 23 pmid 3880746 issue 1 transferase stub Category EC 2.3.1 Category NADPH dependent enzymes Category Enzymes of unknown structure it Micocerosato sintasi ... more details
enzyme Name chitin synthase EC number 2.4.1.16 CAS number 9030 18 6 IUBMB EC number 2 4 1 16 GO code 0004100 image width caption In enzymology , a chitin synthase EC number 2.4.1.16 is an enzyme that catalysis catalyzes the chemical reaction UDP N acetyl D glucosamine 1,4 N acetyl beta D glucosaminyl n math rightleftharpoons math UDP 1,4 N acetyl beta D glucosaminyl n sup sup 1 Thus, the two substrate biochemistry substrates of this enzyme are UDP N acetyl D glucosamine and 1,4 N acetyl beta D glucosaminyl n , whereas its two product chemistry products are uridine diphosphate UDP and 1,4 N acetyl beta D glucosaminyl n 1 . This enzyme belongs to the family of glycosyltransferase s, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP N acetyl D glucosamine chitin 4 beta N acetylglucosaminyl transferase . Other names in common use include chitin UDP N acetylglucosaminyltransferase , chitin uridine diphosphate acetylglucosaminyltransferase , chitin synthetase , and trans N acetylglucosaminosylase . This enzyme participates in aminosugars metabolism . Production Chitin Synthase is manufactured in the rough endoplasmic reticulum of fungi as the inactive form, zymogen . The zymogen is then packaged into chitosomes in the golgi apparatus . Chitosomes bring the zymogen to the hyphal tip of a mold or yeast cell membrane. Chitin synthase is placed into the interior side of the cell membrane and then activated. Citation needed date October 2011 References reflist 1 cite journal author GLASER L, BROWN DH date 1957 title The synthesis of chitin in cell free extracts of Neurospora crassa journal J. Biol. Chem. volume 228 pages 729&ndash 42 pmid 13475355 issue 2 cite journal author Sburlati A, Cabib E date 1986 title Chitin synthetase 2, a presumptive participant in septum formation in Saccharomyces cerevisiae journal J. Biol. Chem. volume 261 pages 15147&ndash 52 pmid 2945823 issue 32 enzyme stub Category EC 2.4.1 Category Enzymes of unknown structure ... more details
enzyme Name Riboflavin synthase EC number 2.5.1.9 CAS number 9075 82 5 IUBMB EC number 2 5 1 9 GO code ... E. coli br riboflavin synthase. ref name Liao PDB 1i8d Cite journal author Liao DI, Wawrzak Z, Calabrese JC, Viitanen PV, Jordan DB title Crystal structure of riboflavin synthase journal Structure volume ... issn ref Infobox protein family Symbol DMRL synthase Name 6,7 dimethyl 8 ribityllumazine synthase image Monomer With Ligands.jpg width caption Riboflavin synthase from Schizosaccharomyces pombe S. pombe ... AK, Kairies N, Cushman M, Illarionov B, Eisenreich W, Bacher A, Huber R, Steinbacher S, Fischer M title Studies on the reaction mechanism of riboflavin synthase X ray crystal structure of a complex with 6 ... , PDB2 2c9b , PDB2 2c9d , PDB2 2f59 , PDB2 2i0f , PDB2 2o6h , PDB2 2obx , PDB2 2vi5 Riboflavin synthase ... H ,3 H pyrimidinedione Structure The Riboflavin synthase monomer is 23kDa. Each monomer contains two ... fold symmetry, predicted by sequence similarity between the N terminus barrels residues 4 86 and the C ... enzyme ?ec 2.5.1.9&tab assemblies ref Active site Two 6,7 dimethyl 8 ribityllumazine Lumazine synthase ... synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments ... terminal domain and Ser41, Thr50, Gly 62, Ala64, Ser64, Val103, Cys48, His102 at the N terminal domain ... and mechanism of riboflavin synthase journal Arch. Biochem. Biophys. volume 474 issue 2 pages ... C terminal domain. ref name Gerhardt Image Hydrogen Bonding N Terminal Domain.jpg Hydrogen bonding between substrate and enzyme at the N terminus N terminal domain. ref name Gerhardt gallery Mechanism ... synthase. ref name Bacher Cite journal author Bacher A, Eberhardt S, Fischer M, Kis K, Richter ... Thr148 dyad as a base for deprotonation of the C7a methyl group . Of the dyad, His102 is from the N ... synthase journal Bioorg. Chem. volume 31 issue 4 pages 278 87 year 2003 month August pmid 12877878 ..., including riboflavin synthase, can be used to develop antibacterial drugs in order to treat infections ... more details
, Li N, Ke H title Crystal structures of 1 aminocyclopropane 1 carboxylate ACC synthase in complex with aminoethoxyvinylglycine ... and prevent the ACC synthase catalyzed reaction with SAM. ref cite journal author Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H title Crystal structures of 1 aminocyclopropane 1 carboxylate ACC synthase ..., Li N title Tyr152 plays a central role in the catalysis of 1 aminocyclopropane 1 carboxylate synthase ...enzyme Name 1 aminocyclopropane 1 carboxylate synthase EC number 4.4.1.14 CAS number 72506 68 4 IUBMB ... Structure of ACC Synthase File ACCsynthasecomplexwPLP.png thumb 300px ACC Synthase Complex with PLP File ACS & PLP complex with labeled 278 and 152 residues.png thumb 300px ACC Synthase Complex with PLP Catalytic Domain Aminocyclopropane 1 carboxylic acid synthase ACC synthase, ACS EC 4.4.1.14 is an enzyme ... methyl cycle and a useful molecule for methyl transfer. ACC synthase, like other PLP dependent enzymes ... of 1 aminocyclopropane 1 carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ... jbc.M103840200 url ref In enzymology , a 1 aminocyclopropane 1 carboxylate synthase EC number ... use include 1 aminocyclopropanecarboxylate synthase , 1 aminocyclopropane 1 carboxylic acid synthase , 1 aminocyclopropane 1 carboxylate synthetase , aminocyclopropanecarboxylic acid synthase , aminocyclopropanecarboxylate synthase , ACC synthase , and S adenosyl L methionine methylthioadenosine lyase ... by 1 aminocyclopropane 1 carboxylic acid synthase ACS is the committed and rate limiting step in the biosynthesis ... cite journal author Li JF, Qu LH, Li N title Tyr152 plays a central role in the catalysis of 1 aminocyclopropane 1 carboxylate synthase journal J. Exp. Bot. volume 56 issue 418 pages 2203 10 year ... DL, Gut H, Gr tter MG, Kirsch JF title Apple 1 aminocyclopropane 1 carboxylate synthase in complex ... 2002 pmid 12045274 pmc 151252 doi url ref Regulation ACC synthase reaches optimal activity in conditions of pH 8.5 and with Km 20 um relative to its substrate, SAM. ACC Synthase and ethylene biosynthesis ... more details
enzyme Name mannosyl 3 phosphoglycerate synthase EC number 2.4.1.217 CAS number 393512 63 5 IUBMB EC number 2 4 1 217 GO code 0050504 image width caption In enzymology , a mannosyl 3 phosphoglycerate synthase EC number 2.4.1.217 is an enzyme that catalysis catalyzes the chemical reaction GDP mannose 3 phospho D glycerate math rightleftharpoons math GDP 2 alpha D mannosyl 3 phosphoglycerate Thus, the two substrate biochemistry substrates of this enzyme are GDP mannose and 3 phospho D glycerate , whereas its two product chemistry products are guanosine diphosphate GDP and 2 alpha D mannosyl 3 phosphoglycerate . This enzyme belongs to the family of glycosyltransferase s, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP mannose 3 phosphoglycerate 3 alpha D mannosyltransferase . This enzyme is also called MPG synthase . References reflist 1 cite journal author Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS date 2001 title Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes journal J. Biol. Chem. volume 276 pages 43580&ndash 8 pmid 11562374 doi 10.1074 jbc.M108054200 issue 47 enzyme stub Category EC 2.4.1 Category Enzymes of unknown structure ... more details
Enzyme Name Tryptophan Synthase EC number 4.2.1.20 CAS number 9014 52 2 IUBMB EC number 4 2 1 20 GO code 0004834 image Tryptophan Synthase Dimer 3.png width caption Subunits font color blue Alpha Subunit ... font Tryptophan synthase or tryptophan synthetase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan . ref name Tryptophan synthase cite journal author Dunn MF, Niks D, Ngo H, Barends TRM, Schlichting I title Tryptophan synthase the workings of a channeling nanomachine ... cite journal author Jablonski P, Jablonski L, Pintado O, Sriranganathan N, Howde C title Tryptophan synthase Identification of Pasteurella multocida tryptophan synthase B subunit by antisera against ... j.protis.2005.04.001 url issn ref Fungi, ref name Fungi , cite journal author Ireland C, Peekhaus N ... RC, Ko SS, Tong CG, Yang RY, Chan MT title Overexpression of Arabidopsis thaliana tryptophan synthase ... SC, Kubler E, Hoffmann B, Braus GH title The tryptophan synthase encoding trpB gene of Aspergillus ... author Raboni S, Bettati S, Mozzarelli A title Tryptophan synthase a mine for enzymologists journal ... s00018 009 0028 0 url issn ref The active sites of tryptophan synthase are allosterically coupled. ref ... induced conformational changes of tryptophan synthase journal Biochemistry volume 48 issue 41 pages ... Subunits Tryptophan synthase typically exists as an complex. The and subunits have molecular ... synthase journal Biochemistry volume 37 issue 16 pages 5394 406 year 1998 month April pmid 9548921 ... 10.1146 annurev.biochem.70.1.149 url issn ref Image Tryptophan Synthase Mechanism 5.gif thumb left alt caption. Image 2 Proposed Mechanism of Tryptophan Synthase Enzyme Mechanism subunit reaction ... KS, Miles EW, Johnson KA title Serine modulates substrate channeling in tryptophan synthase. A novel ... Catalyzed by Tryptophan Synthase Image Active Site 2.gif thumb center alt caption. Image 1 Active Sites for and Subunits Showing Hypothesized Catalytic Residues Biological Function Tryptophan synthase ... more details
Spermine synthase is an enzyme that converts spermidine into spermine . External links MeshName Spermine synthase EC number 2.5.1.22 Gene SMS Alkyl and aryl transferases Category Enzymes Biochem stub ... more details
PBB geneid 7298 enzyme Name thymidylate synthase EC number 2.1.1.45 CAS number 9031 61 2 IUBMB EC number 2 1 1 45 GO code 0050757 image width caption Pfam box Symbol Thymidylat synt Name Thymidylate synthase image width caption Pfam PF00303 InterPro IPR000398 SMART Prosite PDOC00086 SCOP 1tys TCDB OPM ..., Montfort WR, Jones MO, Finer Moore JS title Atomic structure of thymidylate synthase target for rational ... and functional analysis of the human thymidylate synthase gene journal J. Biol. Chem. volume ... chemotherapeutic drugs. Thymidylate synthase is an enzyme of about 30 to 35 Kd in most species ... is conserved from phages to vertebrates. Thymidylate synthase is induced by a transcription factor LSF TFCP2 and LSF is an oncogene in hepatocellular carcinoma . LSF and Thymidylate synthase plays ..., thymidylate synthetase can be inhibited by the thymidylate synthase inhibitor s such as fluorinated ... Thymidylate synthase See also Antimetabolite Pyrimidine analogues Pyrimidine analogues Thymidylate synthase inhibitor References reflist Further reading refbegin 2 cite journal author Carreras CW, and Santi DV title The Catalytic Mechanism and Structure of Thymidylate Synthase journal Annual Review ... reductase and thymidylate synthase journal Biochim. Biophys. Acta volume 1587 issue 2 3 ... R last6 Bertino first6 JR cite journal author Liu J title Thymidylate synthase as a translational regulator ... last4 Tai first4 N last5 Yan first5 W last6 Farrell first6 M last7 Bailly first7 M last8 Chen first8 ... site specific cleavage of thymidylate synthase mRNA journal Biochim. Biophys. Acta volume 1587 ... synthase as a 5 fluorouracil resistance mechanism journal Biochim. Biophys. Acta volume ... author Costi MP title Structure based studies on species specific inhibition of thymidylate synthase ... Methyltransferases Nucleotide metabolism DEFAULTSORT Thymidylate Synthase Category EC 2.1.1 de Thymidylat Synthase es Timidilato sintasa fr Thymidylate synthase it Timidilato sintasi pl Syntaza tymidylanowa ... more details
Encyclopedia
top
