D-dopachrome decarboxylase
In enzymology, a D-dopachrome decarboxylase (EC 4.1.1.84) is an enzyme that catalyzes the chemical reaction
- D-dopachrome 5,6-dihydroxyindole + CO2
| 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 | ||||||||
| |||||||||
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. 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. doi:10.1006/bbrc.1998.8123. PMID 9480844.
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