EC 4.1.1.84 - D-dopachrome decarboxylase

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IntEnz Enzyme Nomenclature
EC 4.1.1.84

Names

Accepted name:
D-dopachrome decarboxylase
Other names:
phenylpyruvate tautomerase II
D-tautomerase
D-dopachrome tautomerase
D-dopachrome carboxy-lyase
Systematic name:
D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)

Reaction

Comments:

This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-α-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00892
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033981
CAS Registry Number: 184111-06-6
UniProtKB/Swiss-Prot:

References

  1. Odh, G., Hindemith, A., Rosengren, A.M., Rosengren, E. and Rorsman, H.
    Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole.
    Biochem. Biophys. Res. Commun. 197: 619-624 (1994). [PMID: 8267597]
  2. Yoshida, H., Nishihira, J., Suzuki, M. and Hikichi, K.
    NMR characterization of physicochemical properties of rat D-dopachrome tautomerase.
    Biochem. Mol. Biol. Int. 42: 891-899 (1998). [PMID: 9285056]
  3. Sugimoto, H., Taniguchi, M., Nakagawa, A., Tanaka, I., Suzuki, M. and Nishihira, J.
    Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 Å resolution.
    Biochemistry 38: 3268-3279 (1999). [PMID: 10079069]
  4. Nishihira, J., Fujinaga, M., Kuriyama, T., Suzuki, M., Sugimoto, H., Nakagawa, A., Tanaka, I. and Sakai, M.
    Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation.
    Biochem. Biophys. Res. Commun. 243: 538-544 (1998). [PMID: 9480844]

[EC 4.1.1.84 created 2005]