enzyme Name porphobilinogen synthase EC number 4.2.1.24 CAS number 9036 37 7 IUBMB EC number 4 2 1 24 GO code 0004655 image width caption protein Name ALAD Delta aminolevulinic acid dehydratase caption image width HGNCid 395 Symbol ALAD AltSymbols EntrezGene 210 OMIM 125270 RefSeq NM 001003945 UniProt P13716 PDB ECnumber 4.2.1.24 Chromosome 9 Arm q Band 32 LocusSupplementaryData Infobox protein family Symbol ALAD Name ALAD image PDB 1b4k EBI.jpg width caption high resolution crystal structure of a mg2 dependent 5 aminolevulinic acid dehydratase Pfam PF00490 Pfam clan CL0036 InterPro IPR001731 SMART PROSITE PDOC00153 MEROPS SCOP 1aw5 TCDB OPM family OPM protein CAZy CDD Porphobilinogen synthase or ALA dehydratase , or aminolevulinate dehydratase synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid . All natural tetrapyrroles , including heme s, chlorophyll s and vitamin B12 vitamin B sub 12 sub , share porphobilinogen as a common precursor. It catalyzes the second step of the biosynthesis of porphyrin . The porphobilinogen synthase catalyzed reaction is the first common step in the biosynthesis of all biological tetrapyrroles. Porphobilinogen synthase is the prototype morpheein . Deficiency ALA dehydratase deficiency redirects here A deficiency of porphobilinogen synthase is usually acquired rather than hereditary and can be caused by heavy metal poisoning , especially lead poisoning , as the enzyme is very susceptible to inhibition by heavy metals. ref http library.med.utah.edu NetBiochem hi32.htm ALA dehydratase reaction , from NetBiochem at the University of Utah. Last modified 1 5 95 ref Hereditary insufficiency of porphobilinogen synthase is called Aminolevulinic acid dehydratase deficiency porphyria porphobilinogen synthase or ALA dehydratase deficiency poprhyria . It is an extremely rare cause of porphyria , ref ... to this enzyme , rendering it useless. References reflist External links MeshName delta Aminolevulinic ... more details
enzyme Name dethiobiotin synthase EC number 6.3.3.3 CAS number 37259 75 9 IUBMB EC number 6 3 3 3 GO code 0004141 image width caption In enzymology , a dethiobiotin synthase EC number 6.3.3.3 is an enzyme that catalysis catalyzes the chemical reaction ATP 7,8 diaminononanoate CO sub 2 sub math rightleftharpoons math ADP phosphate dethiobiotin The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 7,8 diaminononanoate , and carbon dioxide CO sub 2 sub , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and dethiobiotin . This enzyme belongs to the family of ligase s, specifically the cyclo ligases, which form carbon nitrogen bonds. The systematic name of this enzyme class is 7,8 diaminononanoate carbon dioxide cyclo ligase ADP forming . This enzyme is also called desthiobiotin synthase . This enzyme participates in biotin metabolism . Structural studies As of late 2007, 14 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1A82 , PDB link 1BS1 , PDB link 1BYI , PDB link 1DAD , PDB link 1DAE , PDB link 1DAF , PDB link 1DAG , PDB link 1DAH , PDB link 1DAI , PDB link 1DAK , PDB link 1DAM , PDB link 1DBS , PDB link 1DTS , and PDB link 2QMO . References reflist 1 cite journal author Krell K, Eisenberg MA date 1970 title The purification and properties of dethiobiotin synthetase journal J. Biol. Chem. volume 245 pages 6558&ndash 66 pmid 4921568 issue 24 cite journal author Yang H C, Tani Y and Ogata K date 1970 title Synthesis of biotin vitamers from biotin diaminocarboxylic acid or 7,8 diaminopelargonic acid by a purified enzyme of Pseudomonas graveolens journal Agric. Biol. Chem. volume 34 pages 1748&ndash 1750 doi 10.1271 bbb1961.34.1748 issue 11 ligase stub Category EC 6.3.3 Category Enzymes of known structure ... more details
enzyme Name NAD sup sup synthase EC number 6.3.1.5 CAS number 9032 69 3 IUBMB EC number 6 3 1 5 GO code 0008795 image width caption orphan date October 2009 In enzymology , a NAD sup sup synthase EC number 6.3.1.5 is an enzyme that catalysis catalyzes the chemical reaction ATP deamido NAD sup sup NH sub 3 sub math rightleftharpoons math AMP diphosphate NAD sup sup The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , deamido NAD deamido NAD sup sup , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and nicotinamide adenine dinucleotide NAD sup sup . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is deamido NAD sup sup ammonia ligase AMP forming . Other names in common use include NAD sup sup synthetase , NAD sup sup synthase , nicotinamide adenine dinucleotide synthetase , and diphosphopyridine nucleotide synthetase . This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism . Structural studies As of late 2007, 11 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1WXE , PDB link 1WXF , PDB link 1WXG , PDB link 1WXH , PDB link 1WXI , PDB link 1XNG , PDB link 1XNH , PDB link 2E18 , PDB link 2PZ8 , PDB link 2PZA , and PDB link 2PZB . References reflist 1 cite journal author Spencer RL, Preiss J date 1967 title Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphospyridine nucleotide synthetase from Escherichia coli b journal J. Biol. Chem. volume 242 pages 385&ndash 92 pmid 4290215 issue 3 ligase stub Category EC 6.3.1 Category NADH dependent enzymes Category Enzymes of known structure ... more details
enzyme Name acetolactate synthase EC number 2.2.1.6 CAS number 9027 45 6 IUBMB EC number 2 2 1 6 GO code 0003984 image Acetolactase Synthase.png width caption Crystal structure of Arabidopsis thaliana acetohydroxyacid synthase complexed with a sulfonylurea herbicide, metsulfuron methyl . ref name pmid16407096 PDB 1YHY cite journal author McCourt JA, Pang SS, King Scott J, Guddat LW, Duggleby RG title Herbicide binding sites revealed in the structure of plant acetohydroxyacid synthase journal Proc. Natl. Acad. Sci. U.S.A. volume 103 issue 3 pages 569 73 year 2006 month January pmid 16407096 pmc 1334660 doi 10.1073 pnas.0508701103 url ref protein Name ilvB bacterial acetolactate synthase like caption image width HGNCid 6041 Symbol ILVBL AltSymbols EntrezGene 10994 OMIM 605770 RefSeq NM 176826 ... synthase ALS enzyme also known as acetohydroxy acid synthase, or AHAS is a protein found in plants ... synthase genes maps within the CADASIL critical region journal Genomics volume 38 issue 2 pages 192 ... of acetolactate synthase that was used for the picture on this page was determined using X ... aldehyde or ketone residues. In this case, acetolactase synthase is a transketolase, which moves ... pmid3511034 cite journal author Dailey FE, Cronan JE title Acetohydroxy acid synthase I, a required ... activity Acetolactate synthesis, also known as acetohydroxy acid synthase, is an enzyme specifically ... in the organism. 2 CH sub 3 sub COCOO sup sup acetolactate synthase CH sub 3 sub COCOHCH ... carbonyl triazolinone s SCTs . Regulation Acetolactate synthase consists of three pairs of subunits. Each pair includes a large subunit, which is thought to be responsible for catalysis , and a small subunit for feedback inhibition . Each subunit pair is located on its own operon . Together ... Reflist External links MeshName Acetolactate synthase Ramachandran plot http www.rcsb.org pdb images ... 1YHY Aldehyde ketone transferases Flavoproteins es Acetohidroxi cido sintasa fr Ac tolactate synthase ... more details
sub 1 sub , MTNR1B MT sub 2 sub , & MTNR1C MT sub 3 sub receptors Opioid Delta Opioid receptor , Kappa ... triphosphate ATP , which, in turn, results in decreased activity of cAMP dependent protein kinase ... of the Gq alpha subunit G sub q sub alpha subunit . Types There are several types of G sub i sub ... Reflist External links MeshName Gi alpha Subunit biochem stub GTPases Intracellular signaling peptides ... more details
enzyme Name RNA polymerase subunit kinase EC number 2.7.11.23 CAS number 122097 00 1 IUBMB EC number 2 7 11 23 GO code 0008353 image width caption In enzymology , a RNA polymerase subunit kinase EC number 2.7.11.23 is an enzyme that catalysis catalyzes the chemical reaction ATP DNA directed RNA polymerase math rightleftharpoons math ADP phospho DNA directed RNA polymerase Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and DNA directed RNA polymerase , whereas its two product chemistry products are adenosine diphosphate ADP and phospho DNA directed RNA polymerase . This enzyme belongs to the family of transferase s, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in protein s protein serine threonine kinase s . The systematic name of this enzyme class is ATP DNA directed RNA polymerase phosphotransferase . Other names in common use include CTD kinase , and STK9 . References reflist 1 cite journal author Lee JM, Greenleaf AL date 1989 title A protein kinase that phosphorylates the C terminal repeat domain of the largest subunit of RNA polymerase II journal Proc. Natl. Acad. Sci. U.S.A. volume 86 pages 3624&ndash 8 pmid 2657724 doi 10.1073 pnas.86.10.3624 issue 10 pmc 287190 Category EC 2.7.11 Category Enzymes of unknown structure enzyme stub ... more details
enzyme Name tetrahydrofolylpolyglutamate synthase EC number 6.3.2.17 CAS number 63363 84 8 IUBMB EC number 6 3 2 17 GO code 0004326 image width caption In enzymology , a tetrahydrofolate synthase EC number 6.3.2.17 is an enzyme that catalysis catalyzes the chemical reaction ATP tetrahydropteroyl gamma Glu n L glutamate math rightleftharpoons math ADP phosphate tetrahydropteroyl gamma Glu n sup sup 1 The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , tetrahydropteroyl gamma Glu n , and L glutamate , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and tetrahydropteroyl gamma Glu n 1 . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is tetrahydropteroyl gamma polyglutamate L glutamate gamma ligase ADP forming . Other names in common use include folylpolyglutamate synthase , folate polyglutamate synthetase , formyltetrahydropteroyldiglutamate synthetase , N10 formyltetrahydropteroyldiglutamate synthetase , folylpoly gamma glutamate synthase , folylpolyglutamyl synthetase , folylpoly gamma glutamate synthase , folylpolyglutamate synthetase , folylpoly gamma glutamate synthetase dihydrofolate synthetase , FPGS , tetrahydrofolylpolyglutamate synthase , tetrahydrofolate L glutamate gamma ligase ADP forming , tetrahydropteroyl gamma Glu n L glutamate gamma ligase , and ADP forming . This enzyme participates in folate biosynthesis . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FGS , PDB link 1JBV , PDB link 1JBW , PDB link 2GC5 , PDB link 2GC6 , PDB link 2GCA , and PDB link 2GCB . References reflist 1 cite journal author Cichowicz DJ, Foo SK, Shane B date 1981 title Folylpoly gamma glutamate synthesis by bacteria and mammalian cells journal Mol. Cell ... more details
enzyme Name carnosine synthase EC number 6.3.2.11 CAS number 9023 61 4 IUBMB EC number 6 3 2 11 GO code 0047730 image width caption In enzymology , a carnosine synthase EC number 6.3.2.11 is an enzyme that catalysis catalyzes the chemical reaction ATP L histidine beta alanine math rightleftharpoons math AMP diphosphate carnosine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L histidine , and beta alanine , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and carnosine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is L histidine beta alanine ligase AMP forming . Other names in common use include carnosine synthetase , carnosine anserine synthetase , homocarnosine carnosine synthetase , and carnosine homocarnosine synthetase . This enzyme participates in 4 metabolism metabolic pathways urea cycle and metabolism of amino groups , alanine and aspartate metabolism , histidine metabolism , and beta alanine metabolism . References reflist 1 cite journal author KALYANKAR GD, MEISTER A date 1959 title Enzymatic synthesis of carnosine and related beta alanyl and gamma aminobutyryl peptides journal J. Biol. Chem. volume 234 pages 3210&ndash 8 pmid 14404206 cite journal author Stenesh JJ and Winnick T date 1960 title Carnosine anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of alanyl peptide synthesis journal Biochem. J. volume 77 pages 575&ndash 581 pmid 16748858 issue 3 pmc 1205078 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
enzyme Name glutathione synthase EC number 6.3.2.3 CAS number 9023 62 5 IUBMB EC number 6 3 2 3 GO code 0004363 image width caption In enzymology , a glutathione synthase EC number 6.3.2.3 is an enzyme that catalysis catalyzes the chemical reaction ATP gamma L glutamyl L cysteine glycine math rightleftharpoons math ADP phosphate glutathione The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , gamma L glutamyl L cysteine , and glycine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and glutathione . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is gamma L glutamyl L cysteine glycine ligase ADP forming . Other names in common use include glutathione synthetase , and GSH synthetase . This enzyme participates in glutamate metabolism and glutathione metabolism . At least one compound, Phosphinate is known to enzyme inhibitor inhibit this enzyme . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1GLV , PDB link 1GSA , PDB link 1GSH , PDB link 1M0T , PDB link 1M0W , PDB link 2GLT , and PDB link 2HGS . References reflist 1 cite journal author Law MY and Halliwell B date 1986 title Purification and properties of glutathione synthetase from Spinacia oleracea leaves journal Plant Sci. volume 43 pages 185&ndash 191 doi 10.1016 0168 9452 86 90016 6 issue 3 cite journal author Macnicol PK date 1987 title Homoglutathione and glutathione synthetases of legume seedlings partial purification and substrate specificity journal Plant Sci. volume 53 pages 229&ndash 235 doi 10.1016 0168 9452 87 90159 2 issue 3 ligase stub Category EC 6.3.2 Category Enzymes of known structure ... more details
enzyme Name glutathionylspermidine synthase EC number 6.3.1.8 CAS number 9077 09 2 IUBMB EC number 6 3 1 8 GO code 0008885 image width caption In enzymology , a glutathionylspermidine synthase EC number 6.3.1.8 is an enzyme that catalysis catalyzes the chemical reaction glutathione spermidine ATP math rightleftharpoons math glutathionylspermidine ADP phosphate The 3 substrate biochemistry substrates of this enzyme are glutathione , spermidine , and adenosine triphosphate ATP , whereas its 3 product chemistry products are glutathionylspermidine , adenosine diphosphate ADP , and phosphate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is gamma L glutamyl L cysteinyl glycine spermidine ligase ADP forming spermidine is numbered so that atom N 1 is in the amino group of the aminopropyl part of the molecule . This enzyme is also called glutathione spermidine ligase ADP forming . This enzyme participates in glutathione metabolism . It employs one cofactor biochemistry cofactor , magnesium . 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 2IO7 , PDB link 2IO8 , PDB link 2IO9 , PDB link 2IOA , and PDB link 2IOB . References reflist 1 cite journal author Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH year 1992 title Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata journal Protein. Sci. volume 1 pages 874&ndash 83 pmid 1304372 doi 10.1002 pro.5560010705 issue 7 pmc 2142158 cite journal author Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT year 1995 title Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase amidase journal J. Biol. Chem. volume 270 pages ... more details
enzyme Name discadenine synthase EC number 2.5.1.24 CAS number 74082 52 3 IUBMB EC number 2 5 1 24 GO code 0047870 image width caption In enzymology , a discadenine synthase EC number 2.5.1.24 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine N sub 6 sub Delta sub 2 sub isopentenyl adenine math rightleftharpoons math 5 methylthioadenosine discadenine Thus, the two substrate biochemistry substrates of this enzyme are S adenosyl L methionine and N6 Delta2 isopentenyl adenine , whereas its two product chemistry products are 5 methylthioadenosine and discadenine . This enzyme belongs to the family of transferase s, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S adenosyl L methionine N6 Delta2 isopentenyl adenine 3 3 amino 3 carboxypropyl transferase . Other names in common use include discadenine synthetase , S adenosyl L methionine 6 N Delta2 isopentenyl adenine , and 3 3 amino 3 carboxypropyl transferase . References reflist 1 cite journal author Taya Y, Tanaka Y, Nishimura S date 1978 title Cell free biosynthesis of discadenine, a spore germination inhibitor of Dictyostelium discoideum journal FEBS. Lett. volume 89 pages 326&ndash 8 pmid 566219 doi 10.1016 0014 5793 78 80247 6 issue 2 transferase stub Category EC 2.5.1 Category Enzymes of unknown structure ... 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
enzyme Name dihydrofolate synthase EC number 6.3.2.12 CAS number 37318 62 0 IUBMB EC number 6 3 2 12 GO code 0008841 image width caption In enzymology , a dihydrofolate synthase EC number 6.3.2.12 is an enzyme that catalysis catalyzes the chemical reaction ATP 7,8 dihydropteroate L glutamate math rightleftharpoons math ADP phosphate 7,8 dihydropteroylglutamate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 7,8 dihydropteroate , and L glutamate , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 7,8 dihydropteroylglutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is 7,8 dihydropteroate L glutamate ligase ADP forming . Other names in common use include dihydrofolate synthetase , 7,8 dihydrofolate synthetase , H2 folate synthetase , 7,8 dihydropteroate L glutamate ligase ADP , dihydrofolate synthetase folylpolyglutamate synthetase , folylpoly gamma glutamate synthetase dihydrofolate synthase , FHFS , FHFS FPGS , dihydropteroate L glutamate ligase ADP forming , and DHFS . This enzyme participates in folate biosynthesis . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1W78 , PDB link 1W7K , and PDB link 2BMB . References reflist 1 cite journal author GRIFFIN MJ, BROWN GM date 1964 title THE BIOSYNTHESIS OF FOLIC ACID. III. ENZYMATIC FORMATION OF DIHYDROFOLIC ACID FROM DIHYDROPTEROIC ACID AND OF TETRAHYDROPTEROYLPOLYGLUTAMIC ACID COMPOUNDS FROM TETRAHYDROFOLIC ACID journal J. Biol. Chem. volume 239 pages 310&ndash 6 pmid 14114858 cite journal author Bognar AL, Osborne C, Shane B, Singer SC, Ferone R date 1985 title Folylpoly gamma glutamate synthetase dihydrofolate synthetase Cloning and high expression of the Escherichia coli folC gene ... more details
enzyme Name phosphoribosylformylglycinamidine synthase EC number 6.3.5.3 CAS number 9032 84 2 IUBMB EC number 6 3 5 3 GO code 0004642 image width caption In enzymology , a phosphoribosylformylglycinamidine synthase EC number 6.3.5.3 is an enzyme that catalysis catalyzes the chemical reaction ATP N sub 2 sub formyl N sub 1 sub 5 phospho D ribosyl glycinamide L glutamine H sub 2 sub O math rightleftharpoons math ADP phosphate 2 formamido N sub 1 sub 5 phospho D ribosyl acetamidine L glutamate The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , N2 formyl N1 5 phospho D ribosyl glycinamide , L glutamine , and water H sub 2 sub O , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , 2 formamido N1 5 phospho D ribosyl acetamidine , 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 N2 formyl N1 5 phospho D ribosyl glycinamide L glutamine amido ligase ADP forming . Other names in common use include phosphoribosylformylglycinamidine synthetase , formylglycinamide ribonucloetide amidotransferase , phosphoribosylformylglycineamidine synthetase , FGAM synthetase , FGAR amidotransferase , 5 phosphoribosylformylglycinamide L glutamine amido ligase , ADP forming , 2 N formyl 1 N 5 phospho D ribosyl glycinamide L glutamine , and amido ligase ADP forming . This enzyme participates in purine metabolism . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1T3T , PDB link 1VK3 , PDB link 1VQ3 , PDB link 2HRU , PDB link 2HRY , PDB link 2HS0 , PDB link 2HS3 , and PDB link 2HS4 . References reflist 1 cite journal author MELNICK I, BUCHANAN JM date 1957 ... of known structure de FGAM Synthase ... more details
enzyme Name trypanothione synthase EC number 6.3.1.9 CAS number 130246 69 4 IUBMB EC number 6 3 1 9 GO code 0047479 image Trypanothione Synthase.jpg width caption In enzymology , a trypanothione synthase EC number 6.3.1.9 is an enzyme that catalysis catalyzes the chemical reaction glutathione glutathionylspermidine ATP math rightleftharpoons math N sub 1 sub ,N sub 8 sub bis glutathionyl spermidine ... , and adenosine triphosphate ATP , whereas its 3 product chemistry products are N1,N8 bis ... synthase is found as a 74.4 KDa monomer consisting of 652 residues with two catalytic ... ATP grasp family fold that is usually found in carbon nitrogen ligases. The N terminal domain ..., however further research into the structure of trypanothione synthase must be done in order to fully ... of Trypanothione The main function of trypanothione synthase is to use the free energy generated from ATP hydrolysis to conjugate glutathione and spermidine to form the intermediate of glutathionylspermidine ... the forward and backwards reactions, trypanothione synthase from trypanosoma cruzi was found to have ... for the protein to properly fold. In parasitic kinetoplastids trypanothione synthase activity is key ... synthase through RNA interference caused a reduced growth rate of two fold among trypanosoma brucei ... experiments which observed cell death after knocking out trypanothione synthase, it was shown that after ..., the cells which did not contain working trypanothione synthase had a much higher death rate ... is that first glutathione and Mg sup 2 sup ATP bind to the enzyme in a ternary complex where glutathione becomes activated by ATP and forms glutathionyl phosphate. ref name Comini2 ADP then leaves ... of trypanothione synthase is currently thought to be driven by conformational changes caused by allosteric ... which allow the synthase domain to block the amidase active site are highly conserved ... Targeting trypanothione synthase could be a novel way of preventing and curing these diseases ... 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
enzyme Name aerobactin synthase EC number 6.3.2.27 CAS number 94047 30 0 IUBMB EC number 6 3 2 27 GO code 0050565 image width caption In enzymology , an aerobactin synthase EC number 6.3.2.27 is an enzyme that catalysis catalyzes the chemical reaction 4 ATP citrate 2 N sub 6 sub acetyl N sub 6 sub hydroxy L lysine 2 H sub 2 sub O math rightleftharpoons math 4 ADP 4 phosphate aerobactin The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , citrate , N6 acetyl N6 hydroxy L lysine , and water H sub 2 sub O , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and aerobactin . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is citrate N6 acetyl N6 hydroxy L lysine ligase ADP forming . This enzyme is also called citrate 6 N acetyl 6 N hydroxy L lysine ligase ADP forming . This enzyme participates in lysine degradation . References reflist 1 cite journal author Appanna DL, Grundy BJ, Szczepan EW and Viswanatha T date 1984 title Aerobactin synthesis in a cell free system of Aerobacter aerogenes 62 1 journal Biochim. Biophys. Acta volume 801 pages 437&ndash 443 cite journal author Gibson F, Magrath DI date 1969 title The isolation and characterization of a hydroxamic acid aerobactin formed by Aerobacter aerogenes 62 I journal Biochim. Biophys. Acta. volume 192 pages 175&ndash 84 pmid 4313071 issue 2 cite journal author Maurer PJ and Miller M date 1982 title Microbial iron chelators total synthesis of aerobactin and its constituent amino acid, N6 acetyl N6 hydroxylysine journal J. Am. Chem. Soc. volume 104 pages 3096&ndash 3101 doi 10.1021 ja00375a025 issue 11 cite journal author de Lorenzo V, Bindereif A, Paw BH, Neilands JB date 1986 title Aerobactin biosynthesis and transport genes of plasmid ColV K30 in Escherichia coli K 12 journal J. Bacteriol. volume 165 pages 570&ndash ... more details
enzyme Name phosphoribosylaminoimidazolesuccinocarboxamide synthase EC number 6.3.2.6 CAS number 9023 67 0 IUBMB EC number 6 3 2 6 GO code 0004639 image width caption Notability date March 2009 In enzymology , a phosphoribosylaminoimidazolesuccinocarboxamide synthase EC number 6.3.2.6 is an enzyme that catalysis catalyzes the chemical reaction ATP 5 amino 1 5 phospho D ribosyl imidazole 4 carboxylate L aspartate math rightleftharpoons math ADP phosphate S 2 5 amino 1 5 phospho D ribosyl imidazole 4 carboxamido succinate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 5 amino 1 5 phospho D ribosyl imidazole 4 carboxylate , and L aspartate , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , S 2 5 amino 1 5 phospho D ribosyl imidazole 4 , and carboxamido succinate . This enzyme belongs to the family of ligase s, to be specific those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is 5 amino 1 5 phospho D ribosyl imidazole 4 carboxylate L aspartate ligase ADP forming . Other names in common use include phosphoribosylaminoimidazole succinocarboxamide synthetase , PurC , SAICAR synthetase , 4 N succinocarboxamide 5 aminoimidazole synthetase , 4 N succinylamino carbonyl 5 aminoimidazole ribonucleotide , synthetase , SAICARs , phosphoribosylaminoimidazolesuccinocarboxamide synthetase , and 5 aminoimidazole 4 N succinocarboxamide ribonucleotide synthetase . This enzyme participates in purine metabolism . Structural studies As of late 2007, 10 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1A48 , PDB link 1KUT , PDB link 1OBD , PDB link 1OBG , PDB link 2CNQ , PDB link 2CNU , PDB link 2CNV , PDB link 2GQR , PDB link 2GQS , and PDB link 2H31 . References reflist ... Synthase Category EC 6.3.2 Category Enzymes of known structure ligase stub ... more details
Infobox protein family Symbol ATP cone Name ATP cone image PDB 7r1r EBI.jpg width caption ribonucleotide reductase e441q mutant r1 protein from escherichia coli Pfam PF03477 Pfam clan InterPro IPR005144 SMART PROSITE MEROPS SCOP 7r1r TCDB OPM family OPM protein CAZy CDD In molecular biology, the ATP cone is an Evolutionary evolutionarily mobile, ATP binding gene regulation regulatory Protein domain domain which is found in a variety of protein s including ribonucleotide reductases, phosphoglycerate kinases and Transcription genetics transcriptional regulators. ref name pmid10939243 cite journal author Aravind L, Wolf YI, Koonin EV title The ATP cone an evolutionarily mobile, ATP binding regulatory domain journal J. Mol. Microbiol. Biotechnol. volume 2 issue 2 pages 191 4 year 2000 month April pmid 10939243 doi url ref In ribonucleotide reductase protein R1 from Escherichia coli this domain is located at the N terminus, and is composed mostly of Alpha helix helices . ref name pmid8052308 cite journal author Uhlin U, Eklund H title Structure of ribonucleotide reductase protein R1 journal Nature volume 370 issue 6490 pages 533 9 year 1994 month August pmid 8052308 doi 10.1038 370533a0 url ref It forms part of the allosteric Effector biology effector region and contains the general allosteric regulation allosteric activity site in a cleft located at the tip of the N terminal region. ref name pmid9309223 cite journal author Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H title Binding of allosteric effectors to ribonucleotide reductase protein R1 reduction of active site cysteines promotes substrate binding journal Structure volume 5 issue 8 pages 1077 92 year 1997 month August pmid 9309223 doi url ref This site Binding molecular bind s either ATP activating or dATP inhibitory , with the base bound in a hydrophobic pocket and the phosphate s bound ... to affect enzyme activity by altering the relative positions of the two protein subunit subunits of ribonucleotide ... 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
ATP Records may refer to ATP World Tour records , a list of records related to the Association of Tennis Professionals ATP Recordings , a British record label disambig ... 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
enzyme Name GMP synthase br glutamine hydrolyzing EC number 6.3.5.2 CAS number 37318 71 1 IUBMB EC number 6 3 5 2 GO code 0003922 image PDB 1gpm EBI.jpg width caption Crystal structure of GMP synthase. ref name pmid8548458 cite journal author Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL title The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families journal Nat. Struct. Biol. volume 3 issue 1 pages 74 86 year 1996 month January pmid 8548458 doi 10.1038 nsb0196 74 url ref Infobox protein family Symbol GMP synt C Name GMP synthase C terminal domain image PDB 1gpm EBI.jpg width caption escherichia coli gmp synthetase complexed with amp and pyrophosphate Pfam PF00958 Pfam clan InterPro IPR001674 SMART PROSITE PDOC00405 MEROPS SCOP 1gpm TCDB OPM family OPM protein CAZy CDD PBB geneid 8833 Guanine monphosphate synthetase , EC 6.3.5.2 also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate . ref name entrez cite web title Entrez Gene GMPS guanine monphosphate synthetase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8833 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text In the de novo synthesis of purine nucleotides, IMP is the branch point metabolite at which point the pathway diverges to the synthesis of either guanine or adenine nucleotides. In the guanine nucleotide pathway, there are 2 enzymes involved in converting ... , a GMP synthase glutamine hydrolysing EC number 6.3.5.2 is an enzyme that catalysis catalyzes the chemical reaction ATP xanthosine 5 phosphate small L small glutamine H sub 2 sub O math rightleftharpoons ... are adenosine triphosphate ATP , xanthosine 5 phosphate , L glutamine small L small glutamine ... 9 pmid 13563458 issue 1 refend External links MeshName GMP synthase Category EC 6.3.5 Category Enzymes ... more details
JB.00523 06 url ref ATP citrate synthase is composed of two distinct protein subunit subunits . In eukaryotes, ATP citrate synthase is a homotetramer of a single large polypeptide, and is used ... on propionate , while type II hexameric citrate synthase is constitutive. ref name pmid9579066 cite journal author Gerike U, Hough DW, Russell NJ, Dyall Smith ML, Danson MJ title Citrate synthase and 2 methylcitrate synthase structural, functional and evolutionary relationships journal Microbiology Reading, Engl. volume 144 issue 4 pages 929 35 year 1998 month April pmid 9579066 doi url ref ATP citrate synthase also known as ATP citrate lyase catalyse s the MgATP dependent, CoA dependent cleavage ... aldol Claisen condensation followed by the hydrolysis of citryl CoA . Citrate synthase enzymes are found ... synthase using essential dynamics sampling journal J. Mol. Biol. volume 339 issue 3 pages ... hexameric citrate synthase that resists acid inactivation journal Biochemistry volume 45 issue 45 ... synthase biocatalysis catalyses the conversion of oxaloacetate and propanoyl CoA into 2R,3S 2 hydroxybutane ... subunits of ATP citrate lyase from Chlorobium tepidum contribute to catalytic activity journal J. Bacteriol ... ATP citrate lyase is an important component of cell growth and transformation journal Oncogene volume ... more details
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