D-dopachrome decarboxylase

D-dopachrome decarboxylase
Identifiers
EC no.	4.1.1.84
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

The enzyme D-dopachrome decarboxylase (EC 4.1.1.84) catalyzes the chemical reaction

D-dopachrome ${\displaystyle \rightleftharpoons }$ 5,6-dihydroxyindole + 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. Bibcode:1993BBRC..197..619O. 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. doi: 10.1080/15216549700203331 . 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.
• Nishihira J, Fujinaga M, Kuriyama T, Suzuki M, Sugimoto H, Nakagawa 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. Bibcode:1998BBRC..243..538N. doi:10.1006/bbrc.1998.8123. PMID   9480844.