enzyme Name cytosinedeaminase EC number 3.5.4.1 CAS number 9025 05 2 IUBMB EC number 3 5 4 1 GO code 0004131 image width caption In enzymology , a cytosinedeaminase EC number 3.5.4.1 is an enzyme that catalysis catalyzes the chemical reaction cytosine H sub 2 sub O math rightleftharpoons math uracil NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are cytosine and water H sub 2 sub O , whereas its two product chemistry products are uracil and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is cytosine aminohydrolase . This enzyme is also called isocytosine deaminase . This enzyme participates in pyrimidine metabolism . Structural studies As of late 2007, 13 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1K6W , PDB link 1K70 , PDB link 1OX7 , PDB link 1P6O , PDB link 1R9X , PDB link 1R9Y , PDB link 1RA0 , PDB link 1RA5 , PDB link 1RAK , PDB link 1RB7 , PDB link 1UAQ , PDB link 1YSB , and PDB link 1YSD . References reflist 1 cite journal author COHEN SS, BARNER HD date 1957 title The conversion of 5 methyldeoxycytidine to thymidine in vitro and in vivo journal J. Biol. Chem. volume 226 pages 631&ndash 42 pmid 13438848 issue 2 cite journal author Kream J and Chargaff E date 1952 title On the cytosinedeaminase of yeast journal J. Am. Chem. Soc. volume 74 issue 20 pages 5157&ndash 5160 doi 10.1021 ja01140a050 hydrolase stub Category EC 3.5.4 Category Enzymes of known structure ... more details
distinguish cytisine cysteine chembox verifiedrevid 443557332 ImageFile1 Cytosine chemical structure.png ImageSize1 120px ImageFile2 Cytosine 3D balls.png ImageSize2 180px ImageFile3 Cytosine 3D vdW.png ... UHFFFAOYAY MeSHName Cytosine Section2 Chembox Properties Formula C sub 4 sub H sub 5 sub ... Chembox Hazards MainHazards FlashPt Autoignition Cytosine C is one of the four main bases found in DNA ... keto group at position 2 . The nucleoside of cytosine is cytidine . In Watson Crick base pair ing, it forms three hydrogen bonds with guanine . History Cytosine was discovered by Albrecht Kossel ... in the same year. Cytosine recently found use in quantum computation . The first time ... on a two qubit NMRQC Nuclear Magnetic Resonance Quantum Computer based on the cytosine molecule ... ph 2F9801027 doi 10.1063 1.476739 id accessdate 2007 10 18 ref Chemical reactions File Cytosine chemical structure.svg thumb left 100px Cytosine with numbered components. Methylation occurs on carbon nr 5. Cytosine can be found as part of DNA, as part of RNA, or as a part of a nucleotide . As cytidine ... adenosine diphosphate ADP to adenosine triphosphate ATP . In DNA and RNA, cytosine is paired with guanine ... glycosylase, which cleaves a uracil in DNA. Cytosine can also be methylated into 5 methylcytosine by an enzyme ... . Active enzymatic deamination of cytosine or 5 methylcytosine by the APOBEC family of cytosine ... S. title Crosstalk between genetic and epigenetic information through cytosine deamination journal ... R title Prebiotic cytosine synthesis a critical analysis and implications for the origin of life ... fa fr Cytosine gl Citosina ko hi hr Citozin id Sitosina it Citosina he jv Sitosin kk lt Citozinas hu Citozin nl Cytosine ja no Cytosin oc Citosina pl Cytozyna pt Citosina ru simple Cytosine sk Cytoz n sl Citozin sr sh Citozin fi Sytosiini sv Cytosin tr Sitozin uk ur Cytosine vi Cytosine zh ... more details
PBB geneid 978 Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene . ref name pmid8422236 ... cytidine deaminase CDD and its use as a marker of monocyte macrophage differentiation journal ... deaminase journal Biochim Biophys Acta volume 1443 issue 3 pages 323 33 year 1999 month Feb pmid 9878810 pmc doi ref ref name entrez cite web title Entrez Gene CDA cytidine deaminase url http www.ncbi.nlm.nih.gov ... with decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias. ref name entrez cite web title Entrez Gene CDA cytidine deaminase ... R title On the interaction of 3,4,5,6 tetrahydrouridine with human liver cytidine deaminase. journal ... journal author Lalibert J, Momparler RL title Human cytidine deaminase purification of enzyme, cloning ... of the human cytidine deaminase CDA gene to chromosome 1 band p35 p36.2. journal Genomics volume ... by human cytidine deaminase requires the catalytic function of the protein. journal Blood volume ... A, et al. title Intracellular localization of human cytidine deaminase. Identification of a functional ... adenosine deaminase and cytidine deaminase activities in patients with systemic lupus erythematosus ... induced cytidine deaminase deaminates deoxycytidine on single stranded DNA but requires the action of RNase ... Expression of cytidine deaminase mRNA in bone marrow cells from patients with acute leukemia journal ... cytidine deaminase. journal Nucleosides Nucleotides Nucleic Acids volume 22 issue 5 8 pages 1535 ... A, et al. title Human cytidine deaminase understanding the catalytic mechanism. journal Nucleosides ... NCN 120023029 cite journal author Ge Y, Jensen TL, Stout ML, et al. title The role of cytidine deaminase and GATA1 mutations in the increased cytosine arabinoside sensitivity of Down syndrome myeloblasts ... al. title Functional properties of subunit interactions in human cytidine deaminase. journal Protein ... SJ, Fromme JC, Verdine GL title Structure of human cytidine deaminase bound to a potent inhibitor ... more details
enzyme Name ADP deaminase EC number 3.5.4.7 CAS number 9027 79 6 IUBMB EC number 3 5 4 7 GO code 0047629 image width caption In enzymology , an ADP deaminase EC number 3.5.4.7 is an enzyme that catalysis catalyzes the chemical reaction ADP H sub 2 sub O math rightleftharpoons math IDP NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and water H sub 2 sub O , whereas its two product chemistry products are IDP and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ADP aminohydrolase . Other names in common use include adenosine diphosphate deaminase , and adenosinepyrophosphate deaminase . References reflist 1 cite journal author Deutsch A and Nilsson R date 1954 title On the dephosphorylation and deamination of adenosine triphosphate by actomyosin gel journal Acta Chem. Scand. volume 8 pages 1898&ndash 1906 doi 10.3891 acta.chem.scand.08 1898 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name ATP deaminase EC number 3.5.4.18 CAS number 37289 21 7 IUBMB EC number 3 5 4 18 GO code 0047692 image width caption In enzymology , an ATP deaminase EC number 3.5.4.18 is an enzyme that catalysis catalyzes the chemical reaction ATP H sub 2 sub O math rightleftharpoons math ITP NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and water H sub 2 sub O , whereas its two product chemistry products are ITP and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ATP aminohydrolase . This enzyme is also called adenosine triphosphate deaminase . References reflist 1 cite journal author Chung ST, Aida K date Tokyo title Purification and properties of ATP deaminase from Microsporum audouini journal J. volume Biochem. pages 1&ndash 9 pmid 6048966 issue 1 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name pterin deaminase EC number 3.5.4.11 CAS number 9025 04 1 IUBMB EC number 3 5 4 11 GO code 0050228 image width caption In enzymology , a pterin deaminase EC number 3.5.4.11 is an enzyme that catalysis catalyzes the chemical reaction 2 amino 4 hydroxypteridine H sub 2 sub O math rightleftharpoons math 2,4 dihydroxypteridine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are 2 amino 4 hydroxypteridine and water H sub 2 sub O , whereas its two product chemistry products are 2,4 dihydroxypteridine and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 2 amino 4 hydroxypteridine aminohydrolase . This enzyme is also called acrasinase . References reflist 1 cite journal author LEVENBERG B, HAYAISHI O date 1959 title A bacterial pterin deaminase journal J. Biol. Chem. volume 234 pages 955&ndash 61 pmid 13654299 issue 4 cite journal author Rembold H, Simmersbach F date 1969 title Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver journal Biochim. Biophys. Acta. volume 184 pages 589&ndash 96 pmid 5821022 issue 3 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name S adenosylhomocysteine deaminase EC number 3.5.4.28 CAS number 125149 24 8 IUBMB EC number 3 5 4 28 GO code 0050270 image width caption In enzymology , a S adenosylhomocysteine deaminase EC number 3.5.4.28 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L homocysteine H sub 2 sub O math rightleftharpoons math S inosyl L homocysteine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are S adenosyl L homocysteine and water H sub 2 sub O , whereas its two product chemistry products are S inosyl L homocysteine and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S adenosyl L homocysteine aminohydrolase . This enzyme is also called adenosylhomocysteine deaminase . References reflist 1 cite journal author Zulty JJ, Speedie MK date 1989 title Purification and characterization of S adenosylhomocysteine deaminase from streptonigrin producing Streptomyces flocculus journal J. Bacteriol. volume 171 pages 6840&ndash 4 pmid 2592350 issue 12 pmc 210584 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
PBB geneid 270 AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene . ref name pmid1400401 cite journal author Mahnke Zizelman DK, Sabina RL title Cloning of human AMP deaminase isoform ... EntrezGene 270 ref Adenosine monophosphate deaminase is an enzyme that converts adenosine monophosphate ... monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays ... kinase by directly inhibiting AMP deaminase, thereby increasing cellular AMP. ref name pmid21059655 ... of AMP deaminase journal J. Biol. Chem. volume 286 issue 1 pages 1 11 year 2011 month January ... ref Pathology A deficiency is associated with myoadenylate deaminase deficiency . gallery Image AMP ... VW, Griffin JL title Myoadenylate deaminase deficiency a new disease of muscle. journal Science ... Sabina RL, Fishbein WN, Pezeshkpour G, et al. title Molecular analysis of the myoadenylate deaminase ... author Morisaki T, Gross M, Morisaki H, et al. title Molecular basis of AMP deaminase deficiency ... P, et al. title Characterization of the human and rat myoadenylate deaminase genes. journal J. Biol ... title Radioisotopic assay for erythrocyte adenosine 5 monophosphate deaminase. journal Clin. Chim. Acta ... author Mercelis R, Martin JJ, Dehaene I, et al. title Myoadenylate deaminase deficiency in a patient ... Kelemen J, Rice DR, Bradley WG, et al. title Familial myoadenylate deaminase deficiency and exertional ... author Baumeister FA, Gross M, Wagner DR, et al. title Myoadenylate deaminase deficiency with severe ... S, et al. title Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria ... author Hisatome I, Morisaki T, Kamma H, et al. title Control of AMP deaminase 1 binding to myosin ... deaminase activity in Alzheimer s disease brain. journal Neurobiol. Aging volume 19 issue 5 pages ... doi cite journal author Abe M, Higuchi I, Morisaki H, et al. title Myoadenylate deaminase deficiency ... al. title A G468 T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency ... more details
enzyme Name dCTP deaminase EC number 3.5.4.13 CAS number 37289 18 2 IUBMB EC number 3 5 4 13 GO code 0008829 image width caption lowercase In enzymology , a dCTP deaminase EC number 3.5.4.13 is an enzyme that catalysis catalyzes the chemical reaction dCTP H sub 2 sub O math rightleftharpoons math dUTP NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are dCTP and water H sub 2 sub O , whereas its two product chemistry products are dUTP and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is dCTP aminohydrolase . Other names in common use include deoxycytidine triphosphate deaminase , and 5 methyl dCTP deaminase . This enzyme participates in pyrimidine metabolism . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1OGH , PDB link 1PKH , PDB link 1PKJ , PDB link 1PKK , PDB link 1XS1 , PDB link 1XS4 , PDB link 1XS6 , PDB link 2J4H , and PDB link 2J4Q . References reflist 1 cite journal author Tomita F, Takahashi I date 1969 title A novel enzyme, dCTP deaminase, found in Bacillus subtilis infected with phage PBS I journal Biochim. Biophys. Acta. volume 179 pages 18&ndash 27 pmid 4976547 issue 1 hydrolase stub Category EC 3.5.4 Category Enzymes of known structure ... more details
enzyme Name 1 pyrroline 4 hydroxy 2 carboxylate deaminase EC number 3.5.4.22 CAS number 9054 77 7 IUBMB EC number 3 5 4 22 GO code 0047425 image width caption In enzymology , a 1 pyrroline 4 hydroxy 2 carboxylate deaminase EC number 3.5.4.22 is an enzyme that catalysis catalyzes the chemical reaction 1 pyrroline 4 hydroxy 2 carboxylate H sub 2 sub O math rightleftharpoons math 2,5 dioxopentanoate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are 1 pyrroline 4 hydroxy 2 carboxylate and water H sub 2 sub O , whereas its two product chemistry products are 2,5 dioxopentanoate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1 pyrroline 4 hydroxy 2 carboxylate aminohydrolase decyclizing . This enzyme is also called HPC deaminase . This enzyme participates in arginine and proline metabolism . References reflist 1 cite journal author Singh RMM and Adams E date 1965 title Enzymatic deamination of Delta1 pyrroline 4 hydroxy 2 carboxylate to 2,5 dioxovalerate alpha ketoglutaric semialdehyde journal J. Biol. Chem. volume 240 pages 4344&ndash 4351 cite journal author Singh RMM and Adams E date 1965 title Isolation and identification of 2,5 dioxovalerate, an intermediate in the bacterial oxidation of hydroxyproline journal J. Biol. Chem. volume 240 issue 11 pages 4352&ndash 4356 pmid 5845839 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name blasticidin S deaminase EC number 3.5.4.23 CAS number 54576 55 5 IUBMB EC number 3 5 4 23 GO code 0047711 image width caption In enzymology , a blasticidin S deaminase EC number 3.5.4.23 is an enzyme that catalysis catalyzes the chemical reaction blasticidin S H sub 2 sub O math rightleftharpoons math deaminohydroxyblasticidin S NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are blasticidin S and water H sub 2 sub O , whereas its two product chemistry products are deaminohydroxyblasticidin S and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is blasticidin S aminohydrolase . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1WN5 and PDB link 1WN6 . References reflist 1 cite journal author Yamaguchi I, Shibata H, Seto H, Misato T date Tokyo title Isolation and purification of blasticidin S deaminase from Aspergillus terreus journal J. volume Antibiot. pages 7&ndash 14 pmid 236272 issue 1 hydrolase stub Category EC 3.5.4 Category Enzymes of known structure ... more details
enzyme Name guanosine deaminase EC number 3.5.4.15 CAS number 9067 85 0 IUBMB EC number 3 5 4 15 GO code 0047974 image width caption In enzymology , a guanosine deaminase EC number 3.5.4.15 is an enzyme that catalysis catalyzes the chemical reaction guanosine H sub 2 sub O math rightleftharpoons math xanthosine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are guanosine and water H sub 2 sub O , whereas its two product chemistry products are xanthosine and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is guanosine aminohydrolase . This enzyme is also called guanosine aminase . References reflist 1 cite journal author Isihida Y, Shirafiji H, Kida M and Yoneda M date 1969 title Studies on the guanosine degrading system in bacterial cell. III Preparation and properties of guanosine deaminase journal Agric. Biol. Chem. volume 33 pages 384&ndash 390 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name sepiapterin deaminase EC number 3.5.4.24 CAS number 62213 22 3 IUBMB EC number 3 5 4 24 GO code 0050279 image width caption In enzymology , a sepiapterin deaminase EC number 3.5.4.24 is an enzyme that catalysis catalyzes the chemical reaction sepiapterin H sub 2 sub O math rightleftharpoons math xanthopterin B sub 2 sub NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are sepiapterin and water H sub 2 sub O , whereas its two product chemistry products are xanthopterin xanthopterin B2 and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is sepiapterin aminohydrolase . References reflist 1 cite journal author Tsusue M date Tokyo title Studies on sepiapterin deaminase from the silkworm, Bombyx mori Purification and some properties of the enzyme journal J. volume Biochem. pages 781&ndash 8 pmid 5572808 issue 4 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name glucosamine 6 phosphate deaminase EC number 3.5.99.6 CAS number 9013 10 9 IUBMB EC number 3 5 99 6 GO code 0004342 image width caption In enzymology , a glucosamine 6 phosphate deaminase EC number 3.5.99.6 is an enzyme that catalysis catalyzes the chemical reaction D glucosamine 6 phosphate H sub 2 sub O math rightleftharpoons math D fructose 6 phosphate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are glucosamine 6 phosphate and water H sub 2 sub O , whereas its two product chemistry products are fructose 6 phosphate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2 amino 2 deoxy D glucose 6 phosphate aminohydrolase ketol isomerizing . Other names in common use include glucosaminephosphate isomerase , glucosamine 6 phosphate isomerase , phosphoglucosaminisomerase , glucosamine phosphate deaminase , aminodeoxyglucosephosphate isomerase , and phosphoglucosamine isomerase . This enzyme participates in aminosugars metabolism . This enzyme has at least one effector biology effector , N Acetyl D glucosamine 6 phosphate . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1J5X , PDB link 1JT9 , PDB link 1NE7 , PDB link 2BKV , and PDB link 2BKX . References reflist 1 cite journal author COMB DG, ROSEMAN S year 1958 title Glucosamine metabolism. IV. Glucosamine 6 phosphate deaminase journal J. Biol. Chem. volume 232 pages 807&ndash 27 pmid 13549465 issue 2 cite journal author Pattabiraman TN, Bachhawat BK year 1961 title Purification of glucosamine 6 phosphate deaminase from human brain journal Biochim. Biophys. Acta volume 54 pages 273&ndash 283 doi 10.1016 0006 3002 61 90366 3 pmid 14484386 issue 2 ... more details
PBB geneid 100 Infobox protein family Symbol A deaminase Name Adenosine AMP deaminase image PDB 2amx EBI.jpg width caption crystal structure of plasmodium yoelii adenosine deaminase py02076 Pfam PF00962 ... CAZy CDD Infobox protein family Symbol A deamin Name Adenosine deaminase editase domain image width caption crystal structure of the catalytic domain of an adenosine deaminase that acts on rna ... PDOC00419 MEROPS SCOP 1add TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol A deaminase N Name Adenosine AMP deaminase N terminal image width caption crystal structure of human adenosine deaminase growth factor, adenosine deaminase type 2 ada2 complexed with transition state analogue ... OPM protein CAZy CDD Adenosine deaminase also known as adenosine aminhydrolase, or ADA is an enzyme ... Adenonsine deaminase mechanism.jpg thumb Reaction Mechanism at Active Site Two proposed mechanism ... G proteins. ref name eight Pathology Some mutation s in the gene for adenosine deaminase ... mutation in the adenosine deaminase ADA gene implies a high incidence of ADA deficient severe combined ... author Chottiner EG, Cloft HJ, Tartaglia AP, Mitchell BS title Elevated adenosine deaminase activity ... pmid11121182 cite journal author Persico AM, Militerni R, Bravaccio C, et al. title Adenosine deaminase ... of a patient with combined immunodeficiency disease and adenosine deaminase deficiency journal ... deaminase, above 40 U per liter. ref Schwartz s principles of surgery, 8th edition, self assessment and board review, chapter 18 question 16 ref See also Adenosine deaminase deficiency References ... title Adenosine deaminase. A pluridisciplinary enzyme journal Acta m dica portuguesa volume 4 issue .... title Cell surface adenosine deaminase much more than an ectoenzyme journal Prog. Neurobiol. volume ... deaminase binding to human CD26 journal Adv. Exp. Med. Biol. volume 421 issue pages 185 92 ... E, et al. title Presence of adenosine deaminase on the surface of mononuclear blood cells immunochemical ... more details
enzyme Name 1 aminocyclopropane 1 carboxylate deaminase EC number 3.5.99.7 CAS number 69553 48 6 IUBMB EC number 3 5 99 7 GO code 0008660 image width caption In enzymology , a 1 aminocyclopropane 1 carboxylate deaminase EC number 3.5.99.7 is an enzyme that catalysis catalyzes the chemical reaction 1 aminocyclopropane 1 carboxylate H sub 2 sub O math rightleftharpoons math 2 oxobutanoate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are 1 aminocyclopropane 1 carboxylate and water H sub 2 sub O , whereas its two product chemistry products are 2 oxobutanoate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1 aminocyclopropane 1 carboxylate aminohydrolase isomerizing . This enzyme is also called 1 aminocyclopropane 1 carboxylate endolyase deaminating . 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 1RQX , PDB link 1TYZ , PDB link 1TZ2 , PDB link 1TZJ , PDB link 1TZK , and PDB link 1TZM . References reflist 1 cite journal author Honma M and Shimomura T date 1978 title Metabolism of 1 aminocyclopropane 1 carboxylic acid journal Agric. Biol. Chem. volume 42 pages 1825&ndash 1831 cite journal author Wakatsuki S, Yokoi D, Murakami T, Honma M and Tanaka I date 2000 title Crystal structure of 1 aminocyclopropane 1 carboxylate deaminase from Hansenula saturnus journal J. Biol. Chem. volume 275 pages 34557&ndash 34565 doi 10.1074 jbc.M004681200 pmid 10938279 issue 44 hydrolase stub Category EC 3.5.99 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name 2 aminomuconate deaminase EC number 3.5.99.5 CAS number IUBMB EC number 3 5 99 5 GO code 0050540 image width caption In enzymology , a 2 aminomuconate deaminase EC number 3.5.99.5 is an enzyme that catalysis catalyzes the chemical reaction 2 aminomuconate H sub 2 sub O math rightleftharpoons math 4 oxalocrotonate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are 2 aminomuconate and water H sub 2 sub O , whereas its two product chemistry products are 4 oxalocrotonate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2 aminomuconate aminohydrolase . This enzyme participates in tryptophan metabolism . References reflist 1 cite journal author He Z, Spain JC date 1998 title A novel 2 aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45 journal J. Bacteriol. volume 180 pages 2502&ndash 6 pmid 9573204 issue 9 pmc 107194 cite journal author He Z, Spain JC date 1997 title Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45 removal of the amino group from 2 aminomuconic semialdehyde journal Appl. Environ. Microbiol. volume 63 pages 4839&ndash 43 pmid 9471964 issue 12 pmc 168809 hydrolase stub Category EC 3.5.99 Category Enzymes of unknown structure ... more details
enzyme Name adenine deaminase EC number 3.5.4.2 CAS number 9027 68 3 IUBMB EC number 3 5 4 2 GO code 0000034 image width caption In enzymology , an adenine deaminase EC number 3.5.4.2 is an enzyme that catalysis catalyzes the chemical reaction adenine H sub 2 sub O math rightleftharpoons math hypoxanthine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are adenine and water H sub 2 sub O , whereas its two product chemistry products are hypoxanthine and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenine aminohydrolase . Other names in common use include adenase , adenine aminase , and ADase . This enzyme participates in purine 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 2ICS . References reflist 1 cite journal author Blauch M, Koch FC and Hane ME date 1939 title A study of xanthine oxidase of rat blood journal J. Biol. Chem. volume 130 pages 471&ndash 486 cite journal author Heppel LA, Hurwitz J and Horecker BL date 1957 title Adenine deaminase of Azotobacter vinelandii journal J. Am. Chem. Soc. volume 79 pages 630&ndash 633 doi 10.1021 ja01560a033 issue 3 hydrolase stub Category EC 3.5.4 Category Enzymes of known structure ... more details
enzyme Name diaminohydroxyphosphoribosylaminopyrimidine deaminase EC number 3.5.4.26 CAS number 68994 19 4 IUBMB EC number 3 5 4 26 GO code 0008835 image width caption In enzymology , a diaminohydroxyphosphoribosylaminopyrimidine deaminase EC number 3.5.4.26 is an enzyme that catalysis catalyzes the chemical reaction 2,5 diamino 6 hydroxy 4 5 phosphoribosylamino pyrimidine H sub 2 sub O math rightleftharpoons math 5 amino 6 5 phosphoribosylamino uracil NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are 2,5 diamino 6 hydroxy 4 5 phosphoribosylamino pyrimidine and water H sub 2 sub O , whereas its two product chemistry products are 5 amino 6 5 phosphoribosylamino uracil and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds specifically in cyclic amidines . The systematic name of this enzyme class is 2,5 diamino 6 hydroxy 4 5 phosphoribosylamino pyrimidine 2 aminohydrolase . This enzyme participates in riboflavin metabolism . 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 2B3Z , PDB link 2D5N , PDB link 2G6V , PDB link 2HXV , PDB link 2O7P , and PDB link 2OBC . References reflist 1 cite journal author Burrows RB, Brown GM date 1978 title Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin journal J. Bacteriol. volume 136 pages 657&ndash 67 pmid 30756 issue 2 pmc 218591 hydrolase stub Category EC 3.5.4 Category Enzymes of known structure ... more details
enzyme Name creatinine deaminase EC number 3.5.4.21 CAS number 37289 15 9 IUBMB EC number 3 5 4 21 GO code 0047790 image width caption In enzymology , a creatinine deaminase EC number 3.5.4.21 is an enzyme that catalysis catalyzes the chemical reaction creatinine H sub 2 sub O math rightleftharpoons math N methylhydantoin NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are creatinine and water H sub 2 sub O , whereas its two product chemistry products are N methylhydantoin and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase . Other names in common use include creatinine hydrolase , and creatinine desiminase . This enzyme participates in arginine and proline metabolism . References reflist 1 cite journal author Szulmajster J date 1958 title Bacterial degradation of creatinine. II. Creatinine desimidase journal Biochim. Biophys. Acta volume 30 pages 154&ndash 163 doi 10.1016 0006 3002 58 90252 X pmid 13584408 issue 1 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name deoxycytidine deaminase EC number 3.5.4.14 CAS number 37259 56 6 IUBMB EC number 3 5 4 14 GO code 0047844 image width caption In enzymology , a deoxycytidine deaminase EC number 3.5.4.14 is an enzyme that catalysis catalyzes the chemical reaction deoxycytidine H sub 2 sub O math rightleftharpoons math deoxyuridine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are deoxycytidine and water H sub 2 sub O , whereas its two product chemistry products are deoxyuridine and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is deoxycytidine aminohydrolase . This enzyme participates in pyrimidine metabolism . References reflist 1 cite journal author Cohen SS date 1953 title Studies on controlling mechanisms in the metabolism of virus infected bacteria journal Cold Spring Harbour Symp. Quant. Biol. volume 18 pages 221&ndash 235 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
enzyme Name pyrithiamine deaminase EC number 3.5.4.20 CAS number 37289 23 9 IUBMB EC number 3 5 4 20 GO code 0050239 image width caption In enzymology , a pyrithiamine deaminase EC number 3.5.4.20 is an enzyme that catalysis catalyzes the chemical reaction 1 4 amino 2 methylpyrimid 5 ylmethyl 3 beta hydroxyethyl 2 methylpyridinium bromide H sub 2 sub O math rightleftharpoons math 1 4 hydroxy 2 methylpyrimid 5 ylmethyl 3 beta hydroxyethyl 2 methylpyridinium bromide NH sub 3 sub The 3 substrate biochemistry substrates of this enzyme are 1 4 amino 2 methylpyrimid 5 ylmethyl 3 beta hydroxyethyl 2 , methylpyridinium bromide , and water H sub 2 sub O , whereas its 3 product chemistry products are 1 4 hydroxy 2 methylpyrimid 5 ylmethyl 3 beta hydroxyethyl 2 , methylpyridinium bromide , and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1 4 amino 2 methylpyrimid 5 ylmethyl 3 beta hydroxyethyl 2 methy lpyridinium bromide aminohydrolase . References reflist 1 cite journal author Sinha AK, Chatterjee GC date 1968 title Metabolism of pyrithiamine by the pyrithiamine requiring mutant of Staphylococcus aureus journal Biochem. J. volume 107 pages 165&ndash 9 pmid 5641872 issue 2 pmc 1198641 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
PBB geneid 3145 Porphobilinogen deaminase also known as hydroxymethylbilane synthase or uroporphyrinogen I synthase is an enzyme involved in the third step of the metabolism of porphyrin , converting porphobilinogen into hydroxymethylbilane . The enzyme has the unique cofactor dipyrromethane . Defective activity of this enzyme can lead to the disorder acute intermittent porphyria . The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text This gene encodes a member of the hydroxymethylbilane synthase superfamily. The encoded protein is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane. Mutations in this gene are associated with the autosomal dominant disease acute intermittent porphyria ... deaminase gene structure and molecular defects. journal J. Bioenerg. Biomembr. volume 27 issue 2 pages ... in porphobilinogen deaminase gene polymorphisms and mutations causing acute intermittent porphyria ... of seven point mutations in the porphobilinogen deaminase gene in patients with acute intermittent ... G, et al. title High frequency of mutations in exon 10 of the porphobilinogen deaminase gene ... Namba H, Narahara K, Tsuji K, et al. title Assignment of human porphobilinogen deaminase to 11q24.1 ... M title Identification of the most common mutation within the porphobilinogen deaminase gene in Swedish ... intermittent porphyria caused by a C T mutation that produces a stop codon in the porphobilinogen deaminase ... in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent ... deaminase in human erythrocytes purification of two forms with apparent molecular weights of 40 .... title A point mutation G A in exon 12 of the porphobilinogen deaminase gene results in exon skipping ... porphobilinogen deaminase journal Nucleic Acids Res. volume 14 issue 15 pages 5955 68 year 1986 ... more details
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