The Enzyme Database

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EC 1.2.1.32     
Accepted name: aminomuconate-semialdehyde dehydrogenase
Reaction: 2-aminomuconate 6-semialdehyde + NAD+ + H2O = 2-aminomuconate + NADH + 2 H+
For diagram of the later stages of tryptophan catabolism, click here
Other name(s): 2-aminomuconate semialdehyde dehydrogenase; 2-hydroxymuconic acid semialdehyde dehydrogenase; 2-hydroxymuconate semialdehyde dehydrogenase; α-aminomuconic ε-semialdehyde dehydrogenase; α-hydroxymuconic ε-semialdehyde dehydrogenase; 2-hydroxymuconic semialdehyde dehydrogenase
Systematic name: 2-aminomuconate-6-semialdehyde:NAD+ 6-oxidoreductase
Comments: Also acts on 2-hydroxymuconate semialdehyde.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37250-95-6
References:
1.  Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O. and Senoh, S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240 (1965) 740–749. [PMID: 14275130]
[EC 1.2.1.32 created 1972]
 
 
EC 1.13.11.74     
Accepted name: 2-aminophenol 1,6-dioxygenase
Reaction: 2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde
Other name(s): amnA (gene name); amnB (gene name); 2-aminophenol:oxygen 1,6-oxidoreductase (decyclizing)
Systematic name: 2-aminophenol:oxygen 1,6-oxidoreductase (ring-opening)
Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme also has some activity with 2-amino-5-methylphenol and 2-amino-4-methylphenol [1]. The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.76, 2-amino-5-chlorophenol 1,6-dioxygenase [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Takenaka, S., Murakami, S., Shinke, R., Hatakeyama, K., Yukawa, H. and Aoki, K. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272 (1997) 14727–14732. [DOI] [PMID: 9169437]
2.  Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1–8. [DOI] [PMID: 15580337]
3.  Li, D.F., Zhang, J.Y., Hou, Y.J., Liu, L., Hu, Y., Liu, S.J., Wang da, C. and Liu, W. Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 32–43. [DOI] [PMID: 23275161]
[EC 1.13.11.74 created 2013]
 
 
EC 3.5.1.120      
Transferred entry: 2-aminomuconate deaminase (2-hydroxymuconate-forming). Now EC 3.5.99.11, 2-aminomuconate deaminase (2-hydroxymuconate-forming)
[EC 3.5.1.120 created 2016, deleted 2017]
 
 
EC 3.5.99.5     
Accepted name: 2-aminomuconate deaminase
Reaction: 2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate + NH3
Other name(s): amnD (gene name); nbaF (gene name)
Systematic name: 2-aminomuconate aminohydrolase
Comments: 2-Aminomuconate is an intermediate in the bacterial biodegradation of nitrobenzene. The enzyme has been isolated from several species, including Pseudomonas pseudocaligenes JS45, Pseudomonas fluorescens KU-7, Pseudomonas sp. AP3 and Burkholderia cenocepacia J2315. The reaction is spontaneous in acid conditions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 201098-29-5
References:
1.  He, Z and Spain, J.C. Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde. Appl. Environ. Microbiol. 63 (1997) 4839–4843. [PMID: 9471964]
2.  He, Z. and Spain, J.C. A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 180 (1998) 2502–2506. [PMID: 9573204]
3.  Takenaka, S., Murakami, S., Kim, Y.J. and Aoki, K. Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3. Arch. Microbiol. 174 (2000) 265–272. [PMID: 11081795]
4.  Muraki, T., Taki, M., Hasegawa, Y., Iwaki, H. and Lau, P.C. Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl. Environ. Microbiol. 69 (2003) 1564–1572. [DOI] [PMID: 12620844]
[EC 3.5.99.5 created 2000, modified 2012]
 
 
EC 3.5.99.11     
Accepted name: 2-aminomuconate deaminase (2-hydroxymuconate-forming)
Reaction: 2-aminomuconate + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NH3
Glossary: 2-aminomuconate = (2Z,4E)-2-aminohexa-2,4-dienedioate
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
Other name(s): cnbZ (gene name)
Systematic name: 2-aminomuconate aminohydrolase [(2Z,4E)-2-hydroxyhexa-2,4-dienedioate-forming]
Comments: The enzyme, characterized from the bacterium Comamonas testosteroni CNB-1, converts 2-aminomuconate to 2-hydroxyhexa-2,4-dienedioate, unlike the enzymes from Pseudomonas, which produce (3E)-2-oxohex-3-enedioate (see EC 3.5.99.5, 2-aminomuconate deaminase). The enzyme also acts on 2-amino-5-chloromuconate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, L., Wu, J.F., Ma, Y.F., Wang, S.Y., Zhao, G.P. and Liu, S.J. A novel deaminase involved in chloronitrobenzene and nitrobenzene degradation with Comamonas sp. strain CNB-1. J. Bacteriol. 189 (2007) 2677–2682. [DOI] [PMID: 17259310]
[EC 3.5.99.11 created 2016 as EC 3.5.1.120, transferred 2017 to EC 3.5.99.11]
 
 
EC 4.1.1.45     
Accepted name: aminocarboxymuconate-semialdehyde decarboxylase
Reaction: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2
For diagram of the later stages of tryptophan catabolism, click here
Glossary: aminocarboxymuconate semialdehyde = 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
Other name(s): picolinic acid carboxylase; picolinic acid decarboxylase; α-amino-β-carboxymuconate-ε-semialdehade decarboxylase; α-amino-β-carboxymuconate-ε-semialdehyde β-decarboxylase; 2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase; 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase
Systematic name: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming)
Comments: Product rearranges non-enzymically to picolinate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-47-7
References:
1.  Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O. and Senoh, S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240 (1965) 740–749. [PMID: 14275130]
[EC 4.1.1.45 created 1972]
 
 


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