Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.84
Description:D-dopachrome decarboxylase.
Alternative Name: Phenylpyruvate tautomerase II.
D-tautomerase.
D-dopachrome tautomerase.
D-dopachrome carboxy-lyase.
Prosite: PDOC00892;
PDB:
PDBScop
2GDG 8029415; 8041794; 8029415; 8041794; 8029415; 8041794;
1MFI 8029415; 8041794; 8029415; 8041794; 8029415; 8041794;
1MFF 8029415; 8041794; 8029415; 8041794; 8029415; 8041794;
1UIZ 8028497; 8040876; 8028497; 8040876; 8028497; 8040876; 8028497; 8040876;
6C5F 8023707; 8036087; 8023707; 8036087; 8023707; 8036087;
 » show all

Cath: 3.30.429.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.84
BRENDA Enzyme Link: BRENDA 4.1.1.84
KEGG Enzyme Link: KEGG4.1.1.84
BioCyc Enzyme Link: BioCyc 4.1.1.84
ExPASy Enzyme Link: ExPASy4.1.1.84
EC2PDB Enzyme Link: EC2PDB 4.1.1.84
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.84
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.84
IntEnz Enzyme Link: IntEnz 4.1.1.84
MEDLINE Enzyme Link: MEDLINE 4.1.1.84
MSA:

4.1.1.84;

Phylogenetic Tree:

4.1.1.84;

Uniprot:
M-CSA:
RHEA:18441 D-dopachrome + H(+) = 5,6-dihydroxyindole + CO2
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4]1-[CH2;+0:5]-[C;H0;+0:6]2=[CH;+0:7]-[C;H0;+0:8](=[O;H0;+0:9])-[C;H0;+0:10](=[O;H0;+0:11])-[CH;+0:12]=[C;H0;+0:13]-2-[NH;+0:14]-1.[H+;H0:15]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[OH;+0:9]-[c;H0;+0:8]1:[cH;+0:12]:[c;H0;+0:13]2:[nH;+0:14]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6]:2:[cH;+0:7]:[c;H0;+0:10]:1-[OH;+0:11]
Reaction
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References

TitleAuthorsDatePubMed ID
Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation.Nishihira J, Fujinaga M, Kuriyama T, Suzuki M, Sugimoto H, Nakagawa A, Tanaka I, Sakai M1998 Feb 139480844
NMR characterization of physicochemical properties of rat D-dopachrome tautomerase.Yoshida H, Nishihira J, Suzuki M, Hikichi K1997 Aug9285056
Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole.Odh G, Hindemith A, Rosengren AM, Rosengren E, Rorsman H1993 Dec 158267597
Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution.Sugimoto H, Taniguchi M, Nakagawa A, Tanaka I, Suzuki M, Nishihira J1999 Mar 1610079069