enzyme Name pseudouridylatesynthase EC number 4.2.1.70 CAS number 9023 35 2 IUBMB EC number 4 2 1 70 GO code 0004730 image width caption In enzymology , a pseudouridylatesynthase EC number 4.2.1.70 is an enzyme that catalysis catalyzes the chemical reaction uracil D ribose 5 phosphate math rightleftharpoons math pseudouridine 5 phosphate H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are uracil and D ribose 5 phosphate , whereas its two product chemistry products are pseudouridine 5 phosphate and water H sub 2 sub O . This enzyme belongs to the family of lyase s, specifically the hydro lyases, which cleave carbon oxygen bonds. The systematic name of this enzyme class is uracil hydro lyase adding D ribose 5 phosphate pseudouridine 5 phosphate forming . Other names in common use include pseudouridylic acid synthetase , pseudouridine monophosphate synthetase , 5 ribosyluracil 5 phosphate synthetase , pseudouridylate synthetase , upsilonUMP synthetase , and uracil hydro lyase adding D ribose 5 phosphate . This enzyme participates in pyrimidine metabolism . Structural studies As of late 2007, 22 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1DJ0 , PDB link 1K8W , PDB link 1KSK , PDB link 1KSL , PDB link 1KSV , PDB link 1PRZ , PDB link 1QYU , PDB link 1R3E , PDB link 1R3F , PDB link 1SB7 , PDB link 1SGV , PDB link 1SI7 , PDB link 1SZW , PDB link 1V9F , PDB link 1V9K , PDB link 1VIO , PDB link 1XPI , PDB link 1Z2Z , PDB link 1ZE1 , PDB link 1ZE2 , PDB link 1ZL3 , and PDB link 2I82 . References reflist 1 cite journal author HEINRIKSON RL, GOLDWASSER E date 1964 title STUDIES ON THE BIOSYNTHESIS OF 5 RIBOSYLURACIL 5 MONOPHOSPHATE IN TETRAHYMENA PYRIFORMIS journal J. Biol. Chem. volume 239 pages 1177&ndash 87 pmid 14165924 cite journal author Matsushita T, Davis FF date 1971 title Studies on pseudouridylic acid synthetase from various sources journal Biochim. Biophys ... more details
Unreferenced 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 ligase s, with lyase 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
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
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
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 3 deoxy 7 phosphoheptulonate synthase EC number 2.5.1.54 CAS number 9026 94 2 IUBMB EC number 2 5 1 54 GO code 0003849 image width caption Overview DAHP synthase EC number 2.5.1.54 is the first ... npg.els.0001315 ref . Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme. In enzymology , a DAHP synthase EC ... P synthase , DAHP synthase , DS Co , DS Mn , KDPH synthase , KDPH synthetase , deoxy D arabino heptulosonate ... synthase is to catalyze the reaction of phosphoenolpyruvate and D erythrose 4 phosphate to DAHP ... in bacteria, but the only mechanism of regulation found in DAHP synthase found in plants is transcriptional ... of bacteria, DAHP synthase is found as three isoenzymes , each of which are sensitive to one ... 9387 ref . In a study of DAHP synthase sensitive to tyrosine in E. coli, it was determined that the enzyme ... , the first substrate of the reaction catalyzed by DAHP synthase, while the enzyme is inhibited ... of the reaction catalyzed by DAHP synthase when the concentration of tyrosine is above 10 M ref ... DAHP synthase from catalyzing the reaction that forms DAHP. Carbon flow into the shikimate pathway ... of DAHP synthase changed ref name Skikimate Pathway Aromatic Amino Acids and Beyond . Catalytic Activity Metal ions are required in order for DAHP synthase to catalyze reactions ref name Skikimate Pathway Aromatic Amino Acids and Beyond . In DAHP synthase, it has been shown that binding ... monomer of DAHP synthase ref name Metal Ion Cofactor . The reaction catalyzed by DAHP synthase is shown below. Deleted image removed File DAHP synthase reaction2.png thumb left 500px This is the reaction catalyzed by DAHP synthase. Structure Deleted image removed File DAHP synthase quarternary structure.png thumb right 300px This image shows the quarternary structure of DAHP synthase. Deleted image removed File DAHP synthase cartoon quartenary structure.png thumb right 300px This image shows the quarternary ... 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
enzyme Name 1 aminocyclopropane 1 carboxylate synthase EC number 4.4.1.14 CAS number 72506 68 4 IUBMB EC number 4 4 1 14 GO code 0016847 image width caption In enzymology , a 1 aminocyclopropane 1 carboxylate synthase EC number 4.4.1.14 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine math rightleftharpoons math 1 aminocyclopropane 1 carboxylate methylthioadenosine Hence, this enzyme has one substrate biochemistry substrate , S adenosyl L methionine , and two product chemistry products , 1 aminocyclopropane 1 carboxylate and methylthioadenosine . This enzyme belongs to the family of lyase s, specifically carbon sulfur lyases. The systematic name of this enzyme class is S adenosyl L methionine methylthioadenosine lyase 1 aminocyclopropane 1 carboxylate forming . Other names in common 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 . This enzyme participates in propanoate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1B8G , PDB link 1IAX , PDB link 1IAY , PDB link 1M4N , PDB link 1M7Y , and PDB link 1YNU . References reflist 1 cite journal author Boller T, Herner RC and Kende H date 1979 title Assay for and enzymatic formation of an ethylene precursor, 1 aminocyclopropane 1 carboxylic acid journal Planta volume 145 pages 293&ndash 303 doi 10.1007 BF00454455 issue 3 cite journal author Yu YB, Adams DO, Yang SF date 1979 title 1 Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene biosynthesis journal Arch. Biochem. Biophys. volume 198 pages 280&ndash 6 pmid 507845 doi 10.1016 0003 ... 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 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
image Atp synthase.PNG right thumb 300px Molecular model of ATP synthase by X ray diffraction method ATP synthase EC number 3.6.3.14 is an important enzyme that provides energy for the cell to use through ... phosphate P sub i sub which releases energy . The overall reaction sequence is ATP synthase ADP P sub i sub ATP Synthase ATP This energy is often in the form of protium or H , moving down an electrochemical ... 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 of the mitochondria. Image Mitochondrie.svg ... 1 431 ref Oligomycin , an antibiotic, is able to inhibit the F sub O sub unit of ATP synthase. These functional regions consist of different protein subunits refer to tables. F sub 1 sub ATP Synthase ... 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 is a proton pore which is emmbeded ... 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 C C ATP5G1 , ATP5G2 , ATP5G3 ... change in the ATP synthase generated by rotation of the gamma subunit. The research group of John ... Biology Unit also in Cambridge , crystallized the F sub 1 sub catalytic domain of ATP synthase ... thumb 220px right Mechanism of ATP synthase. ATP is shown in red, ADP and phosphate in pink ... 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 ... portion of F sub O sub . The structure of the intact ATP synthase is currently known at low resolution ... 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 year ... . 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 ... 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 ... by an enzyme. 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 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
enzyme Name pinene synthase EC number 4.2.3.14 CAS number IUBMB EC number 4 2 3 14 GO code 0050550 image width caption In enzymology , a pinene synthase EC number 4.2.3.14 is an enzyme that catalysis catalyzes the chemical reaction geranyl diphosphate math rightleftharpoons math pinene diphosphate Hence, this enzyme has one substrate biochemistry substrate , geranyl diphosphate , and two product chemistry products , pinene 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 cyclizing, pinene forming . Other names in common use include beta geraniolene synthase , 1S,5S pinene synthase , and geranyldiphosphate diphosphate lyase pinene 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 21792 pmid 9268308 doi 10.1074 jbc.272.35.21784 issue 35 cite journal author Gijzen M, Lewinsohn E, Croteau R date 1991 title Characterization of the constitutive and wound inducible monoterpene cyclases of grand fir Abies grandis journal Arch. Biochem. Biophys. volume 289 pages 267 273 pmid 1898071 doi 10.1016 0003 9861 91 90471 T issue 2 cite journal author Wagschal KC, Pyun HJ, Coates RM, Croteau R date 1994 title Monoterpene biosynthesis isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage Salvia officinalis journal Arch. Biochem. Biophys. volume 308 pages 477 487 pmid 8109978 doi 10.1006 abbi.1994.1068 issue 2 4.2 enzyme stub Category EC 4.2.3 Category Enzymes of unknown structure ... 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 1990 cite journal author Napoli C, Lemieux C, Jorgensen R title Introduction of a Chimeric Chalcone 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 ... 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
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 ... 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 ... Changes of Citrate Synthase. Eur J Biochem. 120, 155 160 http www.blackwell synergy.com ... more details
Orphan date November 2006 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 S carboxymethylcysteine synthase EC number 4.5.1.5 CAS number 124671 39 2 IUBMB EC number 4 5 1 5 GO code 0050272 image width caption In enzymology , a S carboxymethylcysteine synthase EC number 4.5.1.5 is an enzyme that catalysis catalyzes the chemical reaction 3 chloro L alanine thioglycolate math rightleftharpoons math S carboxymethyl L cysteine chloride Thus, the two substrate biochemistry substrates of this enzyme are 3 chloro L alanine and thioglycolate , whereas its two product chemistry products are S carboxymethyl L cysteine and chloride . This enzyme belongs to the family of lyase s, specifically the class of carbon halide lyases. The systematic name of this enzyme class is 3 chloro L alanine chloride lyase adding thioglycolate S carboxymethyl L cysteine forming . This enzyme is also called S carboxymethyl L cysteine synthase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Kumagai H, Suzuki H, Shigematsu H and Tuchikura T date 1989 title S Carboxymethylcysteine synthase from Escherichia coli journal Agric. Biol. Chem. volume 53 pages 2481&ndash 2487 enzyme stub Category EC 4.5.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name rosmarinate synthase EC number 2.3.1.140 CAS number 117590 80 4 IUBMB EC number 2 3 1 140 GO code 0050266 image width caption In enzymology , a rosmarinate synthase EC number 2.3.1.140 is an enzyme that catalysis catalyzes the chemical reaction caffeoyl CoA 3 3,4 dihydroxyphenyl lactate math rightleftharpoons math CoA rosmarinate Thus, the two substrate biochemistry substrates of this enzyme are caffeoyl CoA and 3 3,4 dihydroxyphenyl lactate , whereas its two product chemistry products are coenzyme A CoA and rosmarinate . 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 caffeoyl CoA 3 3,4 dihydroxyphenyl lactate 2 O caffeoyl transferase . Other names in common use include rosmarinic acid synthase , caffeoyl coenzyme A 3,4 dihydroxyphenyllactic acid , caffeoyltransferase , and 4 coumaroyl CoA 4 hydroxyphenyllactic acid 4 coumaroyl transferase . This enzyme participates in tyrosine metabolism . References reflist 1 cite journal author Petersen M and Alfermann AW date 1988 title Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei hydroxyphenylpyruvate reductase and rosmarinic acid synthase journal Z. Naturforsch. C Biosci. volume 43 pages 501&ndash 504 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Rosmarinato sintasi ... more details
Molybdopterin synthase is an enzyme required to sythesize molybdenum cofactor MoCo from precursor Z now known as cyclic pyranopterin monophosphate . It is heterodimeric and coded for by the MOCS2 gene. ref cite journal last1 Sloan first1 J last2 Kinghorn first2 JR last3 Unkles first3 SE title The two subunits of human molybdopterin synthase evidence for a bicistronic messenger RNA with overlapping reading frames journal Nucleic Acids Research volume 27 issue 3 pages 854 8 year 1999 pmc 148257 pmid 9889283 doi 10.1093 nar 27.3.854 ref References reflist Category Enzymes biochem stub ... 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
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