UROD uroporphyrinogendecarboxylase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 7389 accessdate ref UroporphyrinogenIIIdecarboxylase UroD is a homodimeric ... performed by uroporphyrinogenIIIdecarboxylase. J Phys Chem B 2005 109 18195 200. DOI ...PBB geneid 7389 Uroporphyrinogendecarboxylase , also known as UROD , is an enzyme that in humans is encoded by the UROD gene . ref name entrez cite web title Entrez Gene UROD uroporphyrinogendecarboxylase ... of carboxyl groups from the four acetate side chains of uroporphyrinogenIII to yield coproporphyrinogen ... uroporphyrinogendecarboxylase locus in two patients with hepatoerythropoietic porphyria. journal ... al. title Uroporphyrinogendecarboxylase a splice site mutation causes the deletion of exon 6 in multiple ..., Harrison LM, et al. title A point mutation in the coding region of uroporphyrinogendecarboxylase ... and nucleotide sequence of a complete human uroporphyrinogendecarboxylase cDNA. journal J. Biol. Chem ... MG, Raich N, et al. title Assignment of human uroporphyrinogendecarboxylase URO D to the p34 band ... for human uroporphyrinogendecarboxylase. journal Nucleic Acids Res. volume 15 issue 18 pages 7343 ... B, Beaumont C, et al. title Uroporphyrinogendecarboxylase structural mutant Gly281 Glu in a case ... G281E of the human uroporphyrinogendecarboxylase gene causes both hepatoerythropoietic porphyria ..., Fujita H, Ishida N, et al. title Molecular defects of uroporphyrinogendecarboxylase in a patient ..., Romana M, et al. title Uroporphyrinogendecarboxylase complete human gene sequence and molecular study ... S, Ratnaike S title Five new mutations in the uroporphyrinogendecarboxylase gene identified in families ... Whitby FG, Phillips JD, Kushner JP, Hill CP title Crystal structure of human uroporphyrinogendecarboxylase ... cutanea tarda characterization of seven novel uroporphyrinogendecarboxylase mutations and frequency ..., Sassa S, Ratnaike S title Three new mutations in the uroporphyrinogendecarboxylase gene in familial ... more details
Unreferenced date December 2009 Chembox verifiedrevid 370256222 ImageFile UroporphyrinogenIII skeletal.svg ImageSize IUPACName OtherNames Section1 Chembox Identifiers CASNo 1976 85 8 PubChem 1179 SMILES MeSHName UroporphyrinogenIII Section2 Chembox Properties Formula C sub 40 sub H sub 44 sub N sub 4 sub O sub 16 sub MolarMass 836.795 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition UroporphyrinogenIII is an metabolic intermediate in the biosynthesis of protoporphyrin . It is created by the enzyme uroporphyrinogenIII synthase , and is converted into coproporphyrinogen III by the enzyme uroporphyrinogenIIIdecarboxylase . See also Uroporphyrinogen Image Heme synthesis.png center framed Heme synthesis&mdash note that some reactions occur in the cytoplasm and some in the mitochondrion yellow Tetrapyrroles Heme metabolism intermediates DEFAULTSORT UroporphyrinogenIii Category Tetrapyrroles it Uroporfirinogeno III hu Uroporfirinog n III ja III ... more details
enzyme Name UroporphyrinogenIII synthase EC number 4.2.1.75 CAS number 37340 55 9 IUBMB EC number 4 2 1 75 GO code 0004852 image width caption protein Name UroporphyrinogenIII synthase caption image width HGNCid 12592 Symbol UROS AltSymbols EntrezGene 7390 OMIM 606938 RefSeq NM 000375 UniProt P10746 PDB ECnumber 4.2.1.75 Chromosome 10 Arm q Band 25.2 26.3 LocusSupplementaryData Infobox protein family Symbol HEM4 Name UroporphyrinogenIII synthase HemD image PDB 1wd7 EBI.jpg width caption crystal structure of uroporphyrinogeniii synthase from an extremely thermophilic bacterium thermus thermophilus hb8 wild type, native, form 2 crystal Pfam PF02602 Pfam clan InterPro IPR003754 SMART PROSITE MEROPS SCOP 1jr2 TCDB OPM family OPM protein CAZy CDD UroporphyrinogenIII synthase EC number 4.2.1.75 is an enzyme involved in the metabolism of the cyclic tetrapyrrole compound porphyrin . It is involved in the conversion of hydroxymethyl bilane into uroporphyrinogenIII . This enzyme catalysis catalyses the inversion of the final pyrrole unit ring D of the linear tetrapyrrole molecule, linking it to the first pyrrole unit ring A , thereby generating a large macrocyclic structure, uroporphyrinogenIII. ref name pmid11215515 cite journal author Raux E, Schubert HL, Warren MJ title Biosynthesis of cobalamin vitamin B12 a bacterial conundrum journal Cell. Mol. Life Sci. volume 57 issue 13 14 pages 1880 93 year 2000 month December pmid 11215515 doi 10.1007 PL00000670 url ref The enzyme protein ... title Crystal structure of human uroporphyrinogenIII synthase journal EMBO J. volume 20 issue 21 pages ... of metabolism that results from the markedly deficient activity of uroporphyrinogenIII synthase ... year 2007 pmid 17270473 doi 10.1016 j.bcmd.2006.12.001 url ref External links MeshName UroporphyrinogenIII synthase References reflist Porphyrin biosynthesis enzymes Carbon oxygen lyases lyase stub InterPro content IPR003754 Category EC 4.2.1 de UroporphyrinogenIII Synthase ja III ... more details
Uroporphyrinogens are tetrapyrroles with four propionic acid groups P groups and four acetic acid groups A groups . There are four forms, which vary based upon the arrangements of the P and A groups in clockwise order In the I variety i.e. uroporphyrinogen I , the order repeats four times AP AP AP AP. In the III variety i.e. uroporphyrinogen III , the fourth is reversed AP AP AP PA. This is the most common form. In the synthesis of porphyrin , it is created from hydroxymethyl bilane by the enzyme uroporphyrinogen III synthase , and it is converted into coproporphyrinogen III by the enzyme uroporphyrinogen III decarboxylase . The II and IV varieties can be created synthetically, but do not appear in nature. External links MeshName Uroporphyrinogens Tetrapyrroles Category Biomolecules biochem stub ... more details
chembox verifiedrevid 402052189 ImageFile Uroporphyrinogen I.png ImageSize 200px IUPACName OtherNames Section1 Chembox Identifiers CASNo 1867 62 5 PubChem 440775 SMILES Section2 Chembox Properties Formula C sub 40 sub H sub 44 sub N sub 4 sub O sub 16 sub MolarMass 836.795 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Uroporphyrinogen I is a tetrapyrrole which accumulates in acute intermittent porphyria . Tetrapyrroles Biochem stub Category Tetrapyrroles it Uroporfirinogeno I ja I ... more details
enzyme Name 3 oxolaurate decarboxylase EC number 4.1.1.56 CAS number 37290 49 6 IUBMB EC number 4 1 1 56 GO code 0050410 image width caption In enzymology , a 3 oxolaurate decarboxylase EC number 4.1.1.56 is an enzyme that catalysis catalyzes the chemical reaction 3 oxododecanoate math rightleftharpoons math 2 undecanone CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 3 oxododecanoate , and two product chemistry products , 2 undecanone and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 3 oxododecanoate carboxy lyase 2 undecanone forming . Other names in common use include beta ketolaurate decarboxylase , beta ketoacyl decarboxylase , and 3 oxododecanoate carboxy lyase . References reflist 1 cite journal author FRANKE W, PLATZECK A, EICHHORN G date 1961 title On the knowledge of fatty acid catabolism by mold fungi. III. On a decarboxylase for average beta ketomonocarbonic acids beta ketolaurate decarboxylase journal Arch. Mikrobiol. volume 40 issue 1 pages 73&ndash 93 pmid 13701396 doi 10.1007 BF00408834 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name aconitate decarboxylase EC number 4.1.1.6 CAS number 9025 01 8 IUBMB EC number 4 1 1 6 GO code 0047613 image width caption In enzymology , an aconitate decarboxylase EC number 4.1.1.6 is an enzyme that catalysis catalyzes the chemical reaction cis aconitate math rightleftharpoons math itaconate CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , cis aconitate , and two product chemistry products , itaconate and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is cis aconitate carboxy lyase itaconate forming . Other names in common use include cis aconitic decarboxylase , CAD , cis aconitate carboxy lyase , and cis aconitate carboxy lyase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author BENTLEY R, THIESSEN CP date 1957 title Biosynthesis of itaconic acid in Aspergillus terreus. III. The properties and reaction mechanism of cis aconitic acid decarboxylase journal J. Biol. Chem. volume 226 pages 703&ndash 20 pmid 13438855 issue 2 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name benzoylformate decarboxylase EC number 4.1.1.7 CAS number 9025 00 7 IUBMB EC number 4 1 1 7 GO code 0050695 image width caption In enzymology , a benzoylformate decarboxylase EC number 4.1.1.7 is an enzyme that catalysis catalyzes the chemical reaction benzoylformate H sup sup math rightleftharpoons math benzaldehyde CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , benzoylformate , and two product chemistry products , benzaldehyde and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is benzoylformate carboxy lyase benzaldehyde forming . Other names in common use include phenylglyoxylate decarboxylase , and benzoylformate carboxy lyase . This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation . It employs one cofactor biochemistry cofactor , thiamin diphosphate . 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 1BFD , PDB link 1MCZ , PDB link 1PI3 , PDB link 1PO7 , PDB link 1Q6Z , PDB link 1YNO , PDB link 2FN3 , and PDB link 2FWN . References reflist 1 cite journal author GUNSALUS CF, STANIER RY, GUNSALUS IC date 1953 title The enzymatic conversion of mandelic acid to benzoic acid. III Fractionation and properties of the soluble enzymes journal J. Bacteriol. volume 66 pages 548&ndash 53 pmid 13108854 issue 5 pmc 317432 4.1 enzyme stub Category EC 4.1.1 Category Thiamine enzymes Category Enzymes of known structure ... more details
enzyme Name 2 oxoglutarate decarboxylase EC number 4.1.1.71 CAS number 37205 42 8 IUBMB EC number 4 1 1 71 GO code 0008683 image width caption In enzymology , a 2 oxoglutarate decarboxylase EC number 4.1.1.71 is an enzyme that catalysis catalyzes the chemical reaction 2 oxoglutarate math rightleftharpoons math succinate semialdehyde CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 2 oxoglutarate , and two product chemistry products , succinate semialdehyde and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2 oxoglutarate carboxy lyase succinate semialdehyde forming . Other names in common use include oxoglutarate decarboxylase , alpha ketoglutarate decarboxylase , alpha ketoglutaric decarboxylase , oxoglutarate decarboxylase , pre 2 oxoglutarate decarboxylase , and 2 oxoglutarate carboxy lyase . It employs one cofactor biochemistry cofactor , thiamin diphosphate . References reflist 1 cite journal author Shigeoka S, Onishi T, Maeda K, Nakano Y and Kitaoka S date 1986 title Occurrence of thiamin pyrophosphate dependent 2 oxoglutarate decarboxylase in mitochondria of Euglena gracilis journal FEBS Lett. volume 195 pages 43&ndash 47 doi 10.1016 0014 5793 86 80126 0 4.1 enzyme stub Category EC 4.1.1 Category Thiamine enzymes Category Enzymes of unknown structure ... more details
enzyme Name sulfinoalanine decarboxylase EC number 4.1.1.29 CAS number 62213 10 9 IUBMB EC number 4 1 1 29 GO code 0004782 image width caption In enzymology , a sulfinoalanine decarboxylase EC number 4.1.1.29 is an enzyme that catalysis catalyzes the chemical reaction 3 sulfino L alanine math rightleftharpoons math hypotaurine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 3 sulfino L alanine , and two product chemistry products , hypotaurine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 3 sulfino L alanine carboxy lyase hypotaurine forming . Other names in common use include cysteine sulfinate decarboxylase , L cysteinesulfinic acid decarboxylase , cysteine sulfinate decarboxylase , CADCase CSADCase , CSAD , cysteic decarboxylase , cysteinesulfinic acid decarboxylase , cysteinesulfinate decarboxylase , sulfoalanine decarboxylase , and 3 sulfino L alanine carboxy lyase . This enzyme participates in taurine and hypotaurine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2JIS . References reflist 1 cite journal author Guion Rain M C, Portemer C, Chatagner F date 1975 title Rat liver cysteine sulfinate decarboxylase purification, new appraisal of the molecular weight and determination of catalytic properties journal Biochim. Biophys. Acta. volume 384 pages 265&ndash 76 pmid 236774 issue 1 cite journal author JACOBSEN JG, THOMAS LL, SMITH LH Jr date 1964 title PROPERTIES AND DISTRIBUTION OF MAMMALIAN L CYSTEINE SULFINATE CARBOXY LYASES journal Biochim. Biophys. Acta. volume 85 pages 103&ndash 16 pmid 14159288 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of known ... more details
enzyme Name 6 methylsalicylate decarboxylase EC number 4.1.1.52 CAS number 37289 50 2 IUBMB EC number 4 1 1 52 GO code 0047596 image width caption In enzymology , a 6 methylsalicylate decarboxylase EC number 4.1.1.52 is an enzyme that catalysis catalyzes the chemical reaction 6 methylsalicylate math rightleftharpoons math 3 cresol CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 6 methylsalicylate , and two product chemistry products , 3 cresol and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 6 methylsalicylate carboxy lyase 3 cresol forming . Other names in common use include 6 methylsalicylic acid 2,6 cresotic acid decarboxylase , 6 MSA decarboxylase , and 6 methylsalicylate carboxy lyase . References reflist 1 cite journal author Light RJ date 1969 title 6 methylsalicylic acid decarboxylase from Penicillium patulum journal Biochim. Biophys. Acta. volume 191 pages 430&ndash 8 pmid 5354271 issue 2 doi 10.1016 0005 2744 69 90262 9 cite journal author Vogel G and Lynen F date 1970 title 6 Methylsalicylsaure Decarboxylase journal Naturwissenschaften volume 57 page 664 doi 10.1007 BF00598791 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name diaminopimelate decarboxylase EC number 4.1.1.20 CAS number 9024 75 3 IUBMB EC number 4 1 1 20 GO code 0008836 image width caption In enzymology , a diaminopimelate decarboxylase EC number 4.1.1.20 is an enzyme that catalysis catalyzes the chemical reaction meso 2,6 diaminoheptanedioate math rightleftharpoons math L lysine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , meso 2,6 diaminoheptanedioate , and two product chemistry products , L lysine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is meso 2,6 diaminoheptanedioate carboxy lyase L lysine forming . Other names in common use include diaminopimelic acid decarboxylase , meso diaminopimelate decarboxylase , DAP decarboxylase , and meso 2,6 diaminoheptanedioate carboxy lyase . This enzyme participates in lysine biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1HKV , PDB link 1HKW , PDB link 1KNW , PDB link 1KO0 , PDB link 1TUF , PDB link 1TWI , PDB link 2O0T , and PDB link 2P3E . References reflist cite doi 10.1016 0006 3002 55 90257 2 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name diphosphomevalonate decarboxylase EC number 4.1.1.33 CAS number 9024 66 2 IUBMB EC number 4 1 1 33 GO code 0004163 image width caption In enzymology , a diphosphomevalonate decarboxylase EC number 4.1.1.33 is an enzyme that catalysis catalyzes the chemical reaction ATP R 5 diphosphomevalonate math rightleftharpoons math ADP phosphate isopentenyl diphosphate CO sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and R 5 diphosphomevalonate , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , isopentenyl diphosphate , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is ATP R 5 diphosphomevalonate carboxy lyase adding ATP isopentenyl diphosphate forming . Other names in common use include pyrophosphomevalonate decarboxylase , mevalonate 5 pyrophosphate decarboxylase , pyrophosphomevalonic acid decarboxylase , 5 pyrophosphomevalonate decarboxylase , mevalonate 5 diphosphate decarboxylase , and ATP R 5 diphosphomevalonate carboxy lyase dehydrating . This enzyme participates in biosynthesis of steroids . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FI4 , PDB link 2HK2 , PDB link 2HK3 , and PDB link 2HKE . References reflist 1 cite journal author Bloch K, Chaykin S, Phillips AH and de Waard A date 1959 title Mevalonic acid pyrophosphate and isopentenyl pyrophosphate journal J. Biol. Chem. volume 234 pages 2595&ndash 2604 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure ... more details
File AROMATIC L AMINO ACID DECARBOXYLASE.png enzyme Name phenylalanine decarboxylase EC number 4.1.1.53 CAS number 9075 72 3 IUBMB EC number 4 1 1 53 GO code 0050174 image width caption In enzymology , a phenylalanine decarboxylase EC number 4.1.1.53 is an enzyme that catalysis catalyzes the chemical reaction L phenylalanine math rightleftharpoons math phenylethylamine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L phenylalanine , and two product chemistry products , phenylethylamine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L phenylalanine carboxy lyase phenylethylamine forming . Other names in common use include L phenylalanine decarboxylase , aromatic L amino acid decarboxylase , and L phenylalanine carboxy lyase . This enzyme participates in phenylalanine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author LOVENBERG W, WEISSBACH H, UDENFRIEND S date 1962 title Aromatic L amino acid decarboxylase journal J. Biol. Chem. volume 237 pages 89&ndash 93 pmid 14466899 cite journal author Schulz AR, Oliner L date 1967 title The possible role of thyroid aromatic amino acid decarboxylase in thyroxine biosynthesis journal Life. Sci. volume 6 pages 873&ndash 80 pmid 6034195 doi 10.1016 0024 3205 67 90291 3 issue 8 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name phosphopantothenoylcysteine decarboxylase EC number 4.1.1.36 CAS number 9024 69 5 IUBMB EC number 4 1 1 36 GO code 0004633 image width caption In enzymology , a phosphopantothenoylcysteine decarboxylase EC number 4.1.1.36 is an enzyme that catalysis catalyzes the chemical reaction N R 4 phosphopantothenoyl L cysteine math rightleftharpoons math pantotheine 4 phosphate CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , N R 4 phosphopantothenoyl L cysteine , and two product chemistry products , pantotheine 4 phosphate and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, to be specific the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is N R 4 phosphopantothenoyl L cysteine carboxy lyase pantotheine 4 phosphate forming . Other names in common use include 4 phosphopantotheoylcysteine decarboxylase , 4 phosphopantothenoyl L cysteine decarboxylase , PPC decarboxylase , and N R 4 phosphopantothenoyl L cysteine carboxy lyase . This enzyme participates in pantothenate and coa 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 1MVL , PDB link 1MVN , and PDB link 1QZU . References reflist 1 cite journal author Brown GM date 1958 title Requirement of cytidine triphosphate for the biosynthesis of phosphopantetheine journal J. Am. Chem. Soc. volume 80 pages 3161 3161 doi 10.1021 ja01545a062 issue 12 cite journal author BROWN GM date 1959 title The metabolism of pantothenic acid journal J. Biol. Chem. volume 234 pages 370 8 pmid 13630913 issue 2 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure de Phosphopantothenoylcystein Decarboxylase fr Phosphopantoth noylcyst ine d carboxylase ... more details
enzyme Name oxaloacetate decarboxylase EC number 4.1.1.3 CAS number 9024 98 0 IUBMB EC number 4 1 1 3 GO code 0008948 image width caption Infobox protein family Symbol OAD beta Name Na transporting oxaloacetate decarboxylase beta subunit image width caption Pfam PF03977 Pfam clan CL0064 InterPro IPR005661 SMART PROSITE MEROPS SCOP TCDB 3.B.1 OPM family OPM protein CAZy CDD Infobox protein family Symbol OAD gamma Name Oxaloacetate decarboxylase, gamma chain image width caption Pfam PF04277 Pfam clan InterPro IPR005899 SMART PROSITE MEROPS SCOP TCDB 3.B.1 OPM family OPM protein CAZy CDD Oxaloacetate decarboxylase is a carboxy lyases carboxy lyase involved in the conversion of oxaloacetate into pyruvate . It is categorized under EC number 4.1.1.3 . In some bacteria this enzyme is a trimer , composed of alpha, beta and gamma Protein subunit subunits . ref name pmid9428714 cite journal author Bott M, Pfister K, Burda P, Kalbermatter O, Woehlke G, Dimroth P title Methylmalonyl CoA decarboxylase from Propionigenium modestum cloning and sequencing of the structural genes and purification of the enzyme complex journal Eur. J. Biochem. volume 250 issue 2 pages 590 9 year 1997 month December pmid 9428714 doi url ref ref name pmid2549031 cite journal author Laussermair E, Schwarz E, Oesterhelt D, Reinke H, Beyreuther K, Dimroth P title The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane bound subunits beta and gamma. journal J Biol Chem year 1989 volume 264 issue 25 pages 14710 5 pmid 2549031 doi pmc url ref The beta and gamma subunits are integral membrane proteins . ref name pmid2549031 ref name pmid11802728 cite journal author Schmid M, Wild MR, Dahinden P, Dimroth P title Subunit gamma of the oxaloacetate decarboxylase ... author Dahinden P, Auchli Y, Granjon T et al. title Oxaloacetate decarboxylase of Vibrio cholerae ... links MeshName oxaloacetate decarboxylase Carbon carbon lyases enzyme stub InterPro content IPR005661 ... more details
enzyme Name 5 oxopent 3 ene 1,2,5 tricarboxylate decarboxylase EC number 4.1.1.68 CAS number IUBMB EC number 4 1 1 68 GO code 0018800 image width caption In enzymology , a 5 oxopent 3 ene 1,2,5 tricarboxylate decarboxylase EC number 4.1.1.68 is an enzyme that catalysis catalyzes the chemical reaction 5 oxopent 3 ene 1,2,5 tricarboxylate math rightleftharpoons math 2 oxohept 3 enedioate CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 5 oxopent 3 ene 1,2,5 tricarboxylate, and two product chemistry products , 2 oxohept 3 enedioate and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 5 oxopent 3 ene 1,2,5 tricarboxylate carboxy lyase 2 oxohept 3 enedioate forming . Other names in common use include 5 carboxymethyl 2 oxo hex 3 ene 1,6 dioate decarboxylase , and 5 oxopent 3 ene 1,2,5 tricarboxylate carboxy lyase . This enzyme participates in tyrosine metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1I7O . References reflist 1 cite journal doi 10.1111 j.1432 1033.1981.tb06377.x author Garrido Pertierra A and Cooper RA date 1981 title Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4 hydroxyphenylacetate pathway of Escherichia coli journal Eur. J. Biochem. volume 117 pages 581&ndash 584 pmid 7026235 issue 3 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure ... more details
enzyme Name methionine decarboxylase EC number 4.1.1.57 CAS number 37290 50 9 IUBMB EC number 4 1 1 57 GO code 0050095 image width caption In enzymology , a methionine decarboxylase EC number 4.1.1.57 is an enzyme that catalysis catalyzes the chemical reaction L methionine math rightleftharpoons math 3 methylthiopropanamine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L methionine , and two product chemistry products , 3 methylthiopropanamine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L methionine carboxy lyase 3 methylthiopropanamine forming . Other names in common use include L methionine decarboxylase , and L methionine carboxy lyase . References reflist 1 cite journal author Hagion H and Nakayama K date 1968 title Amino acid metabolism in microorganisms. Part IV. L Methionine decarboxylase produced by Streptomyces strain journal Agric. Biol. Chem. volume 32 pages 727&ndash 733 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name valine decarboxylase EC number 4.1.1.14 CAS number 9031 16 7 IUBMB EC number 4 1 1 14 GO code 0050390 image width caption In enzymology , a valine decarboxylase EC number 4.1.1.14 is an enzyme that catalysis catalyzes the chemical reaction L valine math rightleftharpoons math 2 methylpropanamine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L valine , and two product chemistry products , 2 methylpropanamine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L valine carboxy lyase 2 methylpropanamine forming . Other names in common use include leucine decarboxylase , and L valine carboxy lyase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Sutton CR and King HK date 1962 title Inhibition of leucine decarboxylase by thiol binding reagents journal Arch. Biochem. Biophys. volume 96 pages 360&ndash 370 doi 10.1016 0003 9861 62 90421 6 pmid 13918558 issue 2 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name Acetoacetate decarboxylase EC number 4.1.1.4 CAS number 9025 03 0 IUBMB EC number 4 1 1 4 GO code 0047602 image Acetoacetate decarboxylase biounit 3BH3 with inset.png width caption Acetoacetate decarboxylase dodecamer structure with bound 2 Pentanone bound in its active sites. Infobox protein family Symbol ADC Name Acetoacetate decarboxylase image Acetoacetate decarboxylase.png width caption Crystal structure of tetrameric acetoacetate decarboxylase from Chromobacterium violaceum . ref ... of the electrostatic perturbation in acetoacetate decarboxylase journal Nature volume 459 issue ... , PDB2 3bh2 , PDB2 3bh3 , PDB2 3c8w , PDB2 3cmb Acetoacetate decarboxylase ADC is an enzyme involved ... decarboxylase. Importance of lysine 116 in determining the pKa of active site lysine ... actions of acetoacetate decarboxylase. ref name Nelson Nelson, David, and Michael Cox. Lehninger Principles ... 4339 6 ref Enzymatic Reaction foward enzyme Acetoacetate decarboxylase reverse enzyme substrate acetoacetic ... 75px Activity in bacteria In certain bacteria, acetoacetate decarboxylase is involved in solventogenesis ... of acetone by acetoacetate decarboxylase containing bacteria was utilized in large scale industrial ... year 1986 pmc 373084 pmid 3540574 ref Acetoacetate decarboxylase has been found and studied in the following ... for the existence of mammalian acetoacetate decarboxylase with special reference to human blood serum ... GJ title Mammalian acetoacetate decarboxylase activity. Its distribution in subfractions of human ... decarboxylase is a final irreversible step in the ketone body pathway that supplies the body ... of acetoacetate decarboxylase may be to regulate the concentrations of the other, two 4 carbon ... dia.2005.7.115 ref Under elevated levels of acetoacetate and D hydroxybutyrate, acetoacetate decarboxylase ... diabetes. ref name Galassetti References Reflist External links MeshName acetoacetate decarboxylase ... of Acetoacetate decarboxylase http www.genome.ad.jp dbget bin www bget?ko K01574 KEGG Entry of Acetoacetate ... more details
enzyme Name 4 hydroxyphenylacetate decarboxylase EC number 4.1.1.83 CAS number IUBMB EC number 4 1 1 83 GO code 0043722 image width caption In enzymology , a 4 hydroxyphenylacetate decarboxylase EC number 4.1.1.83 is an enzyme that catalysis catalyzes the chemical reaction 4 hydroxyphenyl acetate H sup sup math rightleftharpoons math 4 methylphenol CO sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are 4 hydroxyphenylacetate and hydrogen ion H sup sup , whereas its two product chemistry products are 4 methylphenol and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 4 hydroxyphenyl acetate carboxy lyase 4 methylphenol forming . Other names in common use include p hydroxyphenylacetate decarboxylase , p Hpd , 4 Hpd , and 4 hydroxyphenylacetate carboxy lyase . References reflist 1 cite journal author D Ari L, Barker HA date 1985 title p Cresol formation by cell free extracts of Clostridium difficile journal Arch. Microbiol. volume 143 pages 311&ndash 2 pmid 3938267 doi 10.1007 BF00411256 issue 3 cite journal author Selmer T, Andrei PI date 2001 title p Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p cresol journal Eur. J. Biochem. volume 268 pages 1363&ndash 72 pmid 11231288 doi 10.1046 j.1432 1327.2001.02001.x issue 5 cite journal author Andrei PI, Pierik AJ, Zauner S, Andrei Selmer LC, Selmer T date 2004 title Subunit composition of the glycyl radical enzyme p hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity journal Eur. J. Biochem. volume 271 pages 2225&ndash 30 pmid 15153112 doi 10.1111 j.1432 1033.2004.04152.x issue 11 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name Diaminobutyrate decarboxylase EC number 4.1.1.86 CAS number IUBMB EC number 4 1 1 86 GO code image width caption Orphan date February 2009 In enzymology , a diaminobutyrate decarboxylase EC number 4.1.1.86 is an enzyme that catalysis catalyzes the chemical reaction L 2,4 diaminobutanoate math rightleftharpoons math propane 1,3 diamine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L 2,4 diaminobutanoate , and two product chemistry products , propane 1,3 diamine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L 2,4 diaminobutanoate carboxy lyase propane 1,3 diamine forming . Other names in common use include DABA DC , L 2,4 diaminobutyrate decarboxylase , and L 2,4 diaminobutanoate carboxy lyase . References reflist 1 cite journal author Yamamoto S, Tsuzaki Y, Tougou K, Shinoda S date 1992 title Purification and characterization of L 2,4 diaminobutyrate decarboxylase from Acinetobacter calcoaceticus journal J. Gen. Microbiol. volume 138 pages 1461&ndash 5 pmid 1512577 issue 7 cite journal author Ikai H, Yamamoto S date 1994 title Cloning and expression in Escherichia coli of the gene encoding a novel L 2,4 diaminobutyrate decarboxylase of Acinetobacter baumannii journal FEMS. Microbiol. Lett. volume 124 pages 225&ndash 8 pmid 7813892 issue 2 cite journal author Ikai H, Yamamoto S date 1997 title Identification and analysis of a gene encoding L 2,4 diaminobutyrate 2 ketoglutarate 4 aminotransferase involved in the 1,3 diaminopropane production pathway in Acinetobacter baumannii journal J. Bacteriol. volume 179 pages 5118&ndash 25 pmid 9260954 issue 16 pmc 179370 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name adenosylmethionine decarboxylase EC number 4.1.1.50 CAS number 9036 20 8 IUBMB EC number 4 1 1 50 GO code 0004014 image width caption protein Name adenosylmethionine decarboxylase 1 caption image width HGNCid 457 Symbol AMD1 AltSymbols EntrezGene 262 OMIM 180980 RefSeq NM 001634 UniProt P17707 PDB ECnumber 4.1.1.50 Chromosome 6 Arm q Band 21 LocusSupplementaryData q22 Infobox protein family Symbol AdoMet dc Name AdoMet decarboxylase image PDB 1tlu EBI.jpg width caption crystal structure of thermotoga maritima s adenosylmethionine decarboxylase Pfam PF02675 Pfam clan InterPro IPR003826 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Adenosylmethionine decarboxylase is an enzyme that catalyzes the conversion of S Adenosyl methionine S adenosyl methionine to S Adenosylmethioninamine S adenosylmethioninamine . Polyamine s such as spermidine and spermine are essential for cell biology cellular cell growth growth under most conditions, being implicated in a large number of cellular processes including DNA, RNA and protein biosynthesis protein synthesis . S adenosylmethionine decarboxylase AdoMetDC plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n propylamine residue required for the synthesis of spermidine and spermine from putrescein. ref name pmid2197977 cite journal author van Poelje PD, Snell EE title Pyruvoyl dependent enzymes journal Annu. Rev. Biochem. volume 59 issue pages 29 59 year 1990 pmid 2197977 doi 10.1146 annurev.bi.59.070190.000333 url ref ref name pmid10047786 cite journal author Pegg AE, Xiong H, Feith DJ, Shantz LM title S adenosylmethionine decarboxylase structure, function and regulation by polyamines journal Biochem. Soc. Trans. volume 26 issue 4 pages 580 6 year 1998 month November pmid 10047786 doi url ref Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a Cofactor biochemistry cofactor rather than the more common pyridoxal 5 phosphate. These protein ... more details
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