Enzyme

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     5. Isomerases
        5.3 Intramolecular oxidoreductases
            5.3.2 Interconverting keto- and enol-groups
ID:5.3.2.6
Description:2-hydroxymuconate tautomerase.
Alternative Name: 4-oxalocrotonate tautomerase.
4-oxalocrotonate isomerase.
Cath: 3.30.429.10; 3.90.850.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.3.2.6
BRENDA Enzyme Link: BRENDA 5.3.2.6
KEGG Enzyme Link: KEGG5.3.2.6
BioCyc Enzyme Link: BioCyc 5.3.2.6
ExPASy Enzyme Link: ExPASy5.3.2.6
EC2PDB Enzyme Link: EC2PDB 5.3.2.6
ExplorEnz Enzyme Link: ExplorEnz 5.3.2.6
PRIAM enzyme-specific profiles Link: PRIAM 5.3.2.6
IntEnz Enzyme Link: IntEnz 5.3.2.6
MEDLINE Enzyme Link: MEDLINE 5.3.2.6
MSA:

5.3.2.6;

Phylogenetic Tree:

5.3.2.6;

Uniprot:
M-CSA:
RHEA:33431 (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[CH;+0:4]=[CH;+0:5]-[CH2;+0:6]-[*:7]>>[*:1]-[C;H0;+0:2](-[OH;+0:3])=[CH;+0:4]-[CH;+0:5]=[CH;+0:6]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Uncovering the protocatechuate 2,3-cleavage pathway genes.Kasai D, Fujinami T, Abe T, Mase K, Katayama Y, Fukuda M, Masai E2009 Nov19717587
Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies.Stivers JT, Abeygunawardana C, Mildvan AS, Hajipour G, Whitman CP, Chen LH1996 Jan 238547260
Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases.Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB1996 Jan 238547259
Catalytic mechanism of 4-oxalocrotonate tautomerase: significances of protein-protein interactions on proton transfer pathways.Wu P, Cisneros GA, Hu H, Chaudret R, Hu X, Yang W2012 Jun 1422417185
4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer.Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP1992 Sep 51339435
Kinetic, stereochemical, and structural effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase.Harris TK, Czerwinski RM, Johnson WH Jr, Legler PM, Abeygunawardana C, Massiah MA, Stivers JT, Whitman CP, Mildvan AS1999 Sep 2110493802
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.Wang SC, Johnson WH Jr, Czerwinski RM, Stamps SL, Whitman CP2007 Oct 2317902707