EC |
1.2.1.85 |
Accepted name: |
2-hydroxymuconate-6-semialdehyde dehydrogenase |
Reaction: |
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+ |
|
For diagram of catechol catabolism (meta ring cleavage), click here |
Glossary: |
2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate |
Other name(s): |
xylG (gene name); praB (gene name) |
Systematic name: |
2-hydroxymuconate-6-semialdehyde:NAD+ oxidoreductase |
Comments: |
This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2, catechol 2,3-dioxygenase), and is an intermediate in the bacterial degradation of several aromatic compounds. Has lower activity with benzaldehyde [1]. Activity with NAD+ is more than 10-fold higher than with NADP+ [3]. cf. EC 1.2.1.32, aminomuconate-semialdehyde dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Inoue, J., Shaw, J.P., Rekik, M. and Harayama, S. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. J. Bacteriol. 177 (1995) 1196–1201. [DOI] [PMID: 7868591] |
2. |
Orii, C., Takenaka, S., Murakami, S. and Aoki, K. Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. strain 10d: A different modified meta-cleavage pathway for 2-aminophenols. Biosci. Biotechnol. Biochem. 70 (2006) 2653–2661. [DOI] [PMID: 17090920] |
3. |
Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758–6768. [DOI] [PMID: 19717587] |
|
[EC 1.2.1.85 created 2012] |
|
|
|
|
EC |
1.13.11.35 |
Accepted name: |
pyrogallol 1,2-oxygenase |
Reaction: |
1,2,3-trihydroxybenzene + O2 = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate |
Glossary: |
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
1,2,3-trihydroxybenzene = pyrogallol |
Other name(s): |
pyrogallol 1,2-dioxygenase; 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (decyclizing) |
Systematic name: |
1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (ring-opening) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78310-68-6 |
References: |
1. |
Groseclose, E.E. and Ribbons, D.W. Metabolism of resorcinylic compounds by bacteria: new pathway for resorcinol catabolism in Azotobacter vinelandii. J. Bacteriol. 146 (1981) 460–466. [PMID: 7217008] |
|
[EC 1.13.11.35 created 1984, modified 2012] |
|
|
|
|
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 |
3.5.99.11 |
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 |
5.3.2.6 |
Accepted name: |
2-hydroxymuconate tautomerase |
Reaction: |
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate |
|
For diagram of catechol catabolism (meta ring cleavage), click here |
Glossary: |
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate |
Other name(s): |
4-oxalocrotonate tautomerase (misleading); 4-oxalocrotonate isomerase (misleading); cnbG (gene name); praC (gene name); xylH (gene name) |
Systematic name: |
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto—enol isomerase |
Comments: |
Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols. The enol form (2Z,4E)-2-hydroxyhexa-2,4-dienedioate is produced as part of this pathway and is converted to the keto form (3E)-2-oxohex-3-enedioate by the enzyme [6]. Another keto form, (4E)-2-oxohex-4-enedioate (4-oxalocrotonate), was originally thought to be produced by the enzyme [1,2] but later shown to be produced non-enzymically [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Whitman, C.P., Aird, B.A., Gillespie, W.R. and Stolowich, N.J. Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol. J. Am. Chem. Soc. 113 (1991) 3154–3162. |
2. |
Whitman, C.P., Hajipour, G., Watson, R.J., Johnson, W.H., Jr., Bembenek, M.E. and Stolowich, N.J. Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase. J. Am. Chem. Soc. 114 (1992) 10104–10110. |
3. |
Subramanya, H.S., Roper, D.I., Dauter, Z., Dodson, E.J., Davies, G.J., Wilson, K.S. and Wigley, D.B. Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. Biochemistry 35 (1996) 792–802. [DOI] [PMID: 8547259] |
4. |
Stivers, J.T., Abeygunawardana, C., Mildvan, A.S., Hajipour, G., Whitman, C.P. and Chen, L.H. Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies. Biochemistry 35 (1996) 803–813. [DOI] [PMID: 8547260] |
5. |
Wang, S.C., Johnson, W.H., Jr., Czerwinski, R.M., Stamps, S.L. and Whitman, C.P. Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions. Biochemistry 46 (2007) 11919–11929. [DOI] [PMID: 17902707] |
6. |
Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758–6768. [DOI] [PMID: 19717587] |
|
[EC 5.3.2.6 created 2012] |
|
|
|
|