Refimprove date June 2007 Cystathionine y synthase CGS is an enzyme which plays an important role in regulating the biosynthesis of methionine in bacteria and plants . External links Cite journal author Hacham Y, Avraham T, Amir R title The N terminal region of Arabidopsis cystathionine gamma synthase plays an important regulatory role in methionine metabolism journal Plant Physiol. volume 128 issue 2 pages 454 62 year 2002 month February pmid 11842149 pmc 148908 doi 10.1104 pp.010819 url http www.plantphysiol.org cgi pmidlookup?view long&pmid 11842149 DEFAULTSORT CystathionineSynthase Category Enzymes Enzyme stub ... more details
Orphan date July 2011 enzyme Name cystathionine gamma synthase EC number 2.5.1.48 CAS number 9030 70 0 IUBMB EC number 2 5 1 48 GO code 0003962 image width caption In enzymology , a cystathionine gamma synthase EC number 2.5.1.48 is an enzyme that catalysis catalyzes the chemical reaction O sub 4 sub succinyl L homoserine L cysteine math rightleftharpoons math L cystathionine succinate Thus, the two substrate biochemistry substrates of this enzyme are O4 succinyl L homoserine and L cysteine , whereas its two product chemistry products are L cystathionine and succinate . 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 O4 succinyl L homoserine L cysteine S 3 amino 3 carboxypropyl transferase . Other names in common use include O succinyl L homoserine succinate lyase adding cysteine , O succinylhomoserine thiol lyase , homoserine O transsuccinylase , O succinylhomoserine synthase , O succinylhomoserine synthetase , cystathioninesynthase , cystathionine synthetase , homoserine transsuccinylase , 4 O succinyl L homoserine L cysteine , and S 3 amino 3 carboxypropyl transferase . This enzyme participates in 4 metabolism metabolic pathways methionine metabolism , cysteine metabolism , selenoamino acid metabolism , and sulfur metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Flavin M, Slaughter C year 1967 title Enzymatic synthesis of homocysteine or methionine directly from O succinyl homoserine journal Biochim. Biophys. Acta. volume 132 pages 400&ndash 5 pmid 5340123 issue 2 cite journal author Kaplan MM, Flavin M year 1966 title Cystathionine gamma synthetase of Salmonella. Catalytic ... MC, Messerschmidt A year 1998 title Crystal structure of Escherichia coli cystathionine gamma synthase ... 2 title Cystathionine gamma synthase from Arabidopsis thaliana purification and biochemical characterization ... more details
PBB geneid 875 Cystathioninesynthase , also known as CBS , is an enzyme EC number 4.2.1.22 that in humans ... homocysteine to cystathionine ref cite web title Entrez Gene CBS cystathionine beta synthase url ... Regulation of human cystathionine beta synthase by S adenosyl L methionine evidence for two catalytically ... homocysteine L cystathionine forming . Other names in common use include beta thionase, cysteine synthase ... of the CBS enzyme. ref name pmid11483494 The human enzyme cystathioninesynthase is a tetrameric ... CG title Redox regulation and reaction mechanism of human cystathionine beta synthase a PLP dependent ... cystathionine beta synthase journal Journal of Inorganic Biochemistry volume 100 issue 12 pages 1988 ... R title Human cystathionine beta synthase is a target for sumoylation journal Biochemistry volume ... activity enzyme Name cystathionine beta synthase EC number 4.2.1.22 CAS number 9023 99 8 IUBMB ... Cysteine metabolism. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma ... and molecular characterization of cystathionine beta synthase and serine acetyltransferase from .... ref name Jhee cite journal author Jhee KH, Kruger WD title The role of cystathionine beta synthase ... producing activity of cystathionine beta synthase journal The Journal of Biological Chemistry volume ... Dynamics of carbon monoxide binding to cystathionine beta synthase journal The Journal of Biological ... syndrome is a medical condition characterized by an overexpression of cystathionine beta synthase CBS and a low level of homocysteine in the blood. It has been speculated that cystathionine beta synthase ... sub , which is a cofactor of CBS. Bioengineering Cystathionine beta synthase CBS is involved in oocyte ..., Shang M, Guo JZ title Localization of cystathionine beta synthase in mice ovaries and its expression ... of cystathionine beta synthase deficient homocystinuria. journal Eur. J. Biochem. volume 74 issue ... J, Packman S, Fowler B, Rosenberg LE title Purification and properties of cystathionine beta synthase ... more details
chembox verifiedrevid 443553935 ImageFile Ref chemboximage correct ?? ImageFile Cystathionine.png ImageName Skeletal formula ImageFile1 Cystathionine 3D balls.png ImageSize1 230px ImageName1 Ball and stick model IUPACName 2 amino 4 2 amino 2 carboxy ethyl thio butanoic acid OtherNames small L small Cystathionine S 2 R 2 Amino 2 carboxyethyl small L small homocysteine Section1 Chembox Identifiers KEGG Ref keggcite correct kegg KEGG C00542 InChI 1 C7H14N2O4S c8 4 6 10 11 1 2 14 3 5 9 7 12 13 h4 5H,1 3,8 9H2, H,10,11 H,12,13 InChIKey ILRYLPWNYFXEMH UHFFFAOYAH ChEMBL Ref ebicite correct EBI ChEMBL 209241 StdInChI Ref stdinchicite correct chemspider StdInChI 1S C7H14N2O4S c8 4 6 10 11 1 2 14 3 5 9 7 12 13 h4 5H,1 3,8 9H2, H,10,11 H,12,13 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey ILRYLPWNYFXEMH UHFFFAOYSA N CASNo Ref cascite correct CAS CASNo 56 88 2 PubChem 834 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 811 ChEBI Ref ebicite correct EBI ChEBI 17755 SMILES O C O C N CSCCC C O O N MeSHName Cystathionine Section2 Chembox Properties Formula C sub 7 sub H sub 14 sub N sub 2 sub O sub 4 sub S MolarMass 222.263 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Cystathionine is an intermediate in the synthesis of cysteine . It is generated from homocysteine and serine by cystathionine beta synthase . It is cleaved into cysteine and ketobutyrate by cystathionine gamma lyase . An excess in the urine is called cystathioninuria . File Cysteine Biosynthesis.png thumb left 150px Cysteine metabolism. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma lyase catalyzes the lower reaction. Amino acid metabolism intermediates biochem stub Category Sulfur amino acids fr Cystathionine ja ... 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
Merge Cystathionine beta lyase date May 2011 Unreferenced date September 2009 Cystathionine beta lyase is an enzyme used in the biosynthesis of methionine . It is not present in humans. It is classified under EC number 4.4.1.8 . See also Cystathionine Carbon sulfur lyases lyase stub Category Enzymes Category Essential amino acids Category Lyases Category Sulfur amino acids ... more details
enzyme Name cystathionine gamma lyase EC number 4.4.1.1 CAS number 9012 96 8 IUBMB EC number 4 4 1 1 GO code 0004123 image Cysteine Biosynthesis.png width caption Cysteine metabolism. Cystathionase catalyzes the lower reaction. Cystathionine gamma lyase or cystathionase is an enzyme which breaks down cystathionine into cysteine and ketobutyrate . Pyridoxal phosphate is a prosthetic group of this enzyme. Cystathionine gamma lyase also catalyses the following elimination reactions L homoserine to form H sub 2 sub O, NH sub 3 sub and 2 oxobutanoate L cystine , producing thiocysteine, pyruvic acid pyruvate and NH sub 3 sub L cysteine producing pyruvate, NH sub 3 sub and H sub 2 sub S In some bacteria and mammal s, including humans, this enzyme takes part in generating hydrogen sulfide . ref name Wang 2010 cite journal author Wang R title Toxic Gas, Lifesaver journal Scientific American volume issue pages 52 year 2010 month March pmid doi url http www.scientificamerican.com article.cfm?id toxic gas lifesaver ref Examples The following cystathionine gamma lyase is expressed in humans protein Name cystathionase cystathionine gamma lyase caption image width HGNCid 2501 Symbol CTH AltSymbols EntrezGene 1491 OMIM 607657 RefSeq NM 001902 UniProt P32929 PDB ECnumber 4.4.1.1 Chromosome 1 Arm p Band 31.1 LocusSupplementaryData Pathology An deficiency is associated with cystathioninuria . See also Cysteine metabolism External links MeshName Cystathionine gamma lyase References Reflist lyase stub Carbon sulfur lyases Amino acid metabolism enzymes ... more details
Merge Cystathionine beta lyase date May 2011 enzyme Name cystathionine beta lyase EC number 4.4.1.8 CAS number 9055 05 4 IUBMB EC number 4 4 1 8 GO code 0004121 image width caption Orphan date February 2009 In enzymology , a cystathionine beta lyase EC number 4.4.1.8 is an enzyme that catalysis catalyzes the chemical reaction L cystathionine H sub 2 sub O math rightleftharpoons math L homocysteine NH sub 3 sub pyruvate Thus, the two substrate biochemistry substrates of this enzyme are L cystathionine and water H sub 2 sub O , whereas its 3 product chemistry products are L homocysteine , ammonia NH sub 3 sub , and pyruvate . 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 cystathionine L homocysteine lyase deaminating pyruvate forming . Other names in common use include beta cystathionase , cystine lyase , cystathionine L homocysteine lyase deaminating , and L cystathionine L homocysteine lyase deaminating . This enzyme participates in 5 metabolism metabolic pathways methionine metabolism , cysteine metabolism , selenoamino acid metabolism , nitrogen metabolism , and sulfur metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1CL1 , PDB link 1CL2 , PDB link 1IBJ , PDB link 2FQ6 , and PDB link 2GQN . References reflist 1 cite journal author Anderson NW and Thompson JF date 1979 title Cystine lyase beta cystathionase from turnip roots journal Phytochemistry journal Phytochemistry volume 18 pages 1953&ndash 1958 doi 10.1016 S0031 9422 00 82710 7 issue 12 cite journal author FLAVIN M, SLAUGHTER C date 1964 title CYSTATHIONINE CLEAVAGE ENZYMES OF NEUROSPORA journal J. Biol. Chem. volume 239 pages 2212&ndash 9 pmid 14209950 Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes ... more details
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 ..., Li N, Ke H title Crystal structures of 1 aminocyclopropane 1 carboxylate ACC synthase in complex with aminoethoxyvinylglycine ... 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 ... 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 ... 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 ... 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 ... with ACC synthase, up regulating its activity. However, it is also inhibited by a number of compounds as well. S Adenosylethionine can bind as a substrate for ACC synthase with higher affinity than ... 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
Phytoene synthase is a transferase enzyme involved in the biosynthesis of carotenoid s. It catalyzes the conversion of geranylgeranyl pyrophosphate to phytoene . ref http www.curehunter.com public keywordSummaryC073128 phytoene synthase.do Phytoene synthase ref References reflist Category EC 2.5.1 transferase stub ... more details
Image DOXP.png thumb 1 Deoxy D xylulose 5 phosphate DXP synthase is an enzyme in the non mevalonate pathway . It generates 1 deoxy D xylulose 5 phosphate from pyruvate and glyceraldehyde 3 phosphate . It is classified under EC number 2.2.1.7 . External links MeshName DXP synthase Aldehyde ketone transferases Non mevalonate pathway enzymes Category EC 2.2.1 transferase stub ... 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
Orphan date September 2011 Infobox protein family Symbol DHBP synthase Name DHBP synthase image PDB 1g58 EBI.jpg width caption crystal structure of 3,4 dihydroxy 2 butanone 4 phosphate synthase gold derivative Pfam PF00926 Pfam clan InterPro IPR000422 SMART PROSITE MEROPS SCOP 1iez TCDB OPM family OPM protein CAZy CDD In molecular biology, 3,4 dihydroxy 2 butanone 4 phosphate synthase DHBP synthase RibB EC number 4.1.99.12 is an enzyme which catalysis catalyses the conversion of ribulose 5 phosphate D ribulose 5 phosphate to formate and 3,4 dihydroxy 2 butanone 4 phosphate , the latter serving as the biosynthetic precursor for the xylene ring of riboflavin . ref name pmid9211332 cite journal author Richter G, Krieger C, Volk R, Kis K, Ritz H, Gotze E, Bacher A title Biosynthesis of riboflavin 3,4 dihydroxy 2 butanone 4 phosphate synthase journal Meth. Enzymol. volume 280 issue pages 374 82 year 1997 pmid 9211332 doi 10.1016 S0076 6879 97 80128 0 url ref In Photobacterium leiognathi , the riboflavin synthesis genes ribB DHBP synthase , ribE riboflavin synthase , ribH lumazone synthase and ribA GTP cyclohydrolase II all reside in the lux operon . ref name pmid11396941 cite journal author Lin JW, Chao YF, Weng SF title Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi journal Biochem. Biophys. Res. Commun. volume 284 issue 3 pages 587 95 year 2001 month June pmid 11396941 doi 10.1006 bbrc.2001.5013 url ref RibB is sometimes found as a bifunctional enzyme with GTP cyclohydrolase II that catalyses the first committed step in the biosynthesis of riboflavin. No sequence biology sequence s with significant homology to DHBP synthase are found in the metazoa . References reflist InterPro content IPR000422 Category Protein families ... more details
image Atp synthase.PNG right thumb 300px Molecular model of ATP synthase by X ray diffraction method enzyme Name atp synthase EC number 3.6.3.14 IUBMB EC number 3 6 3 14 CAS number 9000 83 3 GO code 0046961 image width caption ATP synthase EC number 3.6.3.14 is an important enzyme that provides energy ... is ATP synthase ADP P sub i sub ATP Synthase ATP Energy is often released in the form of protium ... within the mitochondria , ATP synthase consists of 2 regions the F sub O sub portion is within the membrane. The F sub 1 sub portion of the ATP synthase is above the membrane, inside the matrix ... sub unit of ATP synthase. These functional regions consist of different protein subunits refer to tables. F sub 1 sub ATP Synthase structure The F sub 1 sub particle is large and can be seen in the transmission .... class wikitable style text align center F sub 1 sub ATP SYNTHASE SUBUNITS Subunit Human Gene ATP synthase alpha beta subunits alpha ATP5A1 , ATPAF2 ATP synthase alpha beta subunits beta ATP5B , ATPAF1 , C16orf7 ATP synthase gamma subunit gamma ATP5C1 ATP synthase delta subunit delta ATP5D ATP synthase epsilon ATP5E F sub O sub ATP Synthase Structure The F sub O sub region of ATP synthase ... ATP8 8 or A6L . class wikitable style text align center F sub O sub ATP SYNTHASE MAIN SUBUNITS Subunit Human Gene ATP synthase subunits A A ATP6 ATP synthase subunit B B ATP5F1 ATP synthase subunit ... is coupled with a conformational change in the ATP synthase generated by rotation of the gamma subunit ..., crystallized the F sub 1 sub catalytic domain of ATP synthase. The structure, at the time the largest ... of ATP synthase. ATP is shown in red, ADP and phosphate in pink, and the rotating subunit in black ... of proton s through the membrane via the F sub O sub region of ATP synthase. A portion of the F sub O sub the ring of ATP synthase subunit C c subunits Rotating locomotion in living systems rotates as the protons pass through the membrane. The ATP synthase subunit C c ring is tightly attached ... 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
protein Name spermidine synthase caption image width HGNCid 11296 Symbol SRM AltSymbols SRML1 EntrezGene 6723 OMIM 182891 RefSeq NM 003132 UniProt P19623 PDB ECnumber 2.5.1.16 Chromosome 1 Arm p Band 36 LocusSupplementaryData p22 Spermidine synthase is an enzyme EC number 2.5.1.16 that transferase catalyzes the transfer of the propylamine group from S Adenosylmethioninamine S adenosylmethioninamine to putrescine in the biosynthesis of spermidine . The enzyme has a molecular weight of approximately 73,000 kD and is composed of two subunits of equal size. See also Adenosylmethionine decarboxylase External links MeshName Spermidine synthase transferase stub Alkyl and aryl transferases Category EC 2.5.1 ... 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 T, Becker A, Sch nbrunn E title Molecular basis for the glyphosate insensitivity of the reaction of 5 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 ... 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 3 dehydroquinate synthase EC number 4.2.3.4 CAS number 37211 77 1 IUBMB EC number 4 2 3 4 GO code 0003856 image 3 dehydroquinate synthase 3CLH.png width caption Ribbon representation of the Helicobacter pylori 3 dehydroquinate synthase. ref name pmid18503755 PDB 3CLH cite journal author Liu ... pylori dehydroquinate synthase journal Biochem. Biophys. Res. Commun. volume 373 issue 1 pages 1 7 ... Pfam box Symbol DHQ synthase Name 3 dehydroquinate synthase image width caption Pfam PF01761 InterPro ... synthase EC number 4.2.3.4 is an enzyme that catalysis catalyzes the chemical reaction 3 deoxy arabino ... in the biosynthesis of aromatic amino acids. 3 dehydroquinate synthase belongs to the family ... catalyzed by 3 dehydroquinate synthase Background The shikimate pathway is composed of seven steps ... to aromatic amino acids. 3 dehydroquinate synthase is the enzyme that catalyzes reaction ... deoxy D arabino heptulosonate 7 phosphate which results in 3 dehydroquinate. 3 dehydroquinate synthase ... ref 3 dehydroquinate synthase is activated by inorganic phosphate, and requires Nicotinamide .... ref name pmid15012217 Function 3 dehydroquinate synthase utilizes a complex multi step ... ML, Parker EJ title Expression, Purification, and Characterisation of Dehydroquinate Synthase from ... 3092513 doi 10.4061 2011 134893 ref Dehydroquinate synthase requires NAD and a cobalt cofactor to catalyze .... ref name pmid21603259 In addition, dehydroquinate synthase is of particular interest because of its ... synthase catalyzes the second step in the shikimate pathway, which is essential for the production ... of Helicobacter pylori dehydroquinate synthase journal Biochem. Biophys. Res. Commun. volume 373 issue ... synthase EPSP synthase which ultimately blocks the production of aromatic amino acids , and without ... synthase which was not inhibited by Roundup. Monsanto introduced this gene into plants using agrobacterium ... synthase shows the arrangement of the secondary structure of the protein File 3 dehydroquinate synthase ... more details
enzyme Name myrcene synthase EC number 4.2.3.15 CAS number IUBMB EC number 4 2 3 15 GO code 0050551 image width caption In enzymology , a myrcene synthase EC number 4.2.3.15 is an enzyme that catalysis catalyzes the chemical reaction geranyl diphosphate math rightleftharpoons math myrcene diphosphate Hence, this enzyme has one substrate biochemistry substrate , geranyl diphosphate , and two product chemistry products , myrcene 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 myrcene forming . This enzyme participates in monoterpenoid biosynthesis . References reflist 1 cite journal author Bohlmann J, Steele CL, Croteau R date 1997 title Monoterpene synthases from grand fir Abies grandis . cDNA isolation, characterization, and functional expression of myrcene synthase, 4S limonene synthase, and 1S,5S pinene synthase journal J. Biol. Chem. volume 272 pages 21784&ndash 92 pmid 9268308 doi 10.1074 jbc.272.35.21784 issue 35 4.2 enzyme stub Category EC 4.2.3 Category Enzymes of unknown structure ... more details
enzyme Name 2 ethylmalate synthase EC number 2.3.3.6 CAS number 9024 01 5 IUBMB EC number 2 3 3 6 GO code 0050438 image width caption In enzymology , a 2 ethylmalate synthase EC number 2.3.3.6 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA H sub 2 sub O 2 oxobutanoate math rightleftharpoons math R 2 ethylmalate CoA The 3 substrate biochemistry substrates of this enzyme are acetyl CoA , water H sub 2 sub O , and 2 oxobutanoate , whereas its two product chemistry products are R 2 ethylmalate 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 acetyl CoA 2 oxobutanoate C acetyltransferase thioester hydrolysing, carboxymethyl forming . Other names in common use include R 2 ethylmalate 2 oxobutanoyl lyase CoA acetylating , 2 ethylmalate 3 hydroxybutanedioate synthase , propylmalate synthase , and propylmalic synthase . This enzyme participates in pyruvate metabolism . References reflist 1 cite journal author Strassman M, Ceci LN date 1967 title A study of acetyl CoA condensation with alpha keto acids journal Arch. Biochem. Biophys. volume 119 pages 420&ndash 8 pmid 6052435 doi 10.1016 0003 9861 67 90473 0 issue 1 transferase stub Category EC 2.3.3 Category Enzymes of unknown structure it 2 etilmalato sintasi ... 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
enzyme Name pinosylvin synthase EC number 2.3.1.146 CAS number 72994 49 1 IUBMB EC number 2 3 1 146 GO code 0050198 image width caption In enzymology , a pinosylvin synthase EC number 2.3.1.146 is an enzyme that catalysis catalyzes the chemical reaction 3 malonyl CoA cinnamoyl CoA math rightleftharpoons math 4 CoA pinosylvin 4 CO sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are malonyl CoA and cinnamoyl CoA , whereas its 3 product chemistry products are coenzyme A CoA , pinosylvin , and carbon dioxide CO sub 2 sub . 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 malonyl CoA cinnamoyl CoA malonyltransferase cyclizing . Other names in common use include stilbene synthase , and pine stilbene synthase . This enzyme participates in phenylpropanoid biosynthesis . References reflist 1 cite journal author Gehlert R, Schoppner A and Kindl H date 1990 title Stilbene synthase from seedlings of Pinus sylvestris purification and induction in response to fungal infection journal Mol. Plant Microbe Interaction volume 3 pages 444&ndash 449 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Pinosilvina sintasi ... more details
enzyme Name L 3 cyanoalanine synthase EC number 4.4.1.9 CAS number 9059 53 4 IUBMB EC number 4 4 1 9 GO code 0050017 image width caption Nofootnotes date January 2008 In enzymology , a L 3 cyanoalanine synthase EC number 4.4.1.9 is an enzyme that catalysis catalyzes the chemical reaction L cysteine hydrogen cyanide math rightleftharpoons math L 3 cyanoalanine hydrogen sulfide Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and hydrogen cyanide , whereas its two product chemistry products are L 3 cyanoalanine and hydrogen sulfide . 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 cysteine hydrogen sulfide lyase adding hydrogen cyanide L 3 cyanoalanine forming . Other names in common use include beta cyanoalanine synthase , beta cyanoalanine synthetase , beta cyano L alanine synthase , and L cysteine hydrogen sulfide lyase adding HCN . This enzyme participates in cyanoamino acid metabolism . References reflist 1 cite journal author Akopyan TN, Braunstein AE, Goryachenkova EV date 1975 title Beta cyanoalanine synthase purification and characterization journal Proc. Natl. Acad. Sci. U.S.A. volume 72 pages 1617&ndash 21 pmid 1055433 doi 10.1073 pnas.72.4.1617 issue 4 pmc 432590 cite journal author Castric PA, Conn EE date 1971 title Formation of cyanoalanine by O acetylserine sulfhydrylase journal J. Bacteriol. volume 108 pages 132&ndash 6 pmid 5001194 issue 1 pmc 247041 cite journal author Hendrickson HR date 1968 title The beta cyanoalanine synthase of blue lupine journal Fed. Proc. volume 27 pages 593 cite journal author Hendrickson HR, Conn EE date 1969 title Cyanide metabolism in higher plants. IV. Purification and properties of the beta cyanolanine synthase of blue lupine journal J. Biol. Chem. volume 244 pages 2632&ndash 40 pmid 5769995 issue 10 enzyme stub Category EC 4.4.1 Category Enzymes of unknown structure ... more details
Encyclopedia
top
