D-dopachrome decarboxylase

D-dopachrome decarboxylase
D-dopachrome decarboxylase
Identifiers
EC number 4.1.1.84
CAS number 184111-06-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

In enzymology, a D-dopachrome decarboxylase (EC 4.1.1.84) is an enzyme that catalyzes the chemical reaction

D-dopachrome \rightleftharpoons 5,6-dihydroxyindole + CO2

Hence, this enzyme has one substrate, D-dopachrome, and two products, 5,6-dihydroxyindole and CO2.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming). Other names in common use include phenylpyruvate tautomerase II, D-tautomerase, D-dopachrome tautomerase, and D-dopachrome carboxy-lyase.

References

  • Odh G, Hindemith A, Rosengren AM, Rosengren E, Rorsman H (1993). "Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole". Biochem. Biophys. Res. Commun. 197 (2): 619–24. doi:10.1006/bbrc.1993.2524. PMID 8267597. 
  • Yoshida H, Nishihira J, Suzuki M, Hikichi K (1997). "NMR characterization of physicochemical properties of rat D-dopachrome tautomerase". Biochem. Mol. Biol. Int. 42 (5): 891–9. PMID 9285056. 
  • J; Taniguchi, M; Nakagawa, A; Tanaka, I; Suzuki, M; Nishihira, J (1999). "Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution". Biochemistry. 38 (11): 3268–79. doi:10.1021/bi982184o. PMID 10079069. 
  • A, Tanaka I, Sakai M (1998). "Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation". Biochem. Biophys. Res. Commun. 243 (2): 538–44. doi:10.1006/bbrc.1998.8123. PMID 9480844. 
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