The Enzyme Database

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EC 4.1.1.84     
Accepted name: D-dopachrome decarboxylase
Reaction: D-dopachrome = 5,6-dihydroxyindole + CO2
Glossary: D-dopachrome = (2R)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate
Other name(s): phenylpyruvate tautomerase II; D-tautomerase; D-dopachrome tautomerase; D-dopachrome carboxy-lyase
Systematic name: D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 184111-06-6
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 (1993) 619–624. [DOI] [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 (1997) 891–899. [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 (1999) 3268–3279. [DOI] [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 (1998) 538–544. [DOI] [PMID: 9480844]
[EC 4.1.1.84 created 2005]
 
 
EC 5.3.3.12     
Accepted name: L-dopachrome isomerase
Reaction: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
For diagram of melanin biosynthesis, click here
Glossary: L-dopachrome = (2S)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate
Other name(s): dopachrome tautomerase; tyrosinase-related protein 2; TRP-1; TRP2; TRP-2; tyrosinase-related protein-2; dopachrome Δ72-isomerase; dopachrome Δ-isomerase; dopachrome conversion factor; dopachrome isomerase; dopachrome oxidoreductase; dopachrome-rearranging enzyme; DCF; DCT; dopachrome keto-enol isomerase; L-dopachrome-methyl ester tautomerase
Systematic name: L-dopachrome keto-enol isomerase
Comments: A zinc enzyme. Stereospecific for L-dopachrome. Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroindole-5,6-quinone) is not (see also EC 4.1.1.84, D-dopachrome decarboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 130122-81-5
References:
1.  Solano, F., Jiménez-Cervantes, C., Martinez-Liarte, J.H., Garcia-Borrón, J.C. and Lozano, J.A. Molecular mechanism for catalysis by a new zinc enzyme, dopachrome tautomerase. Biochem. J. 313 (1996) 447–453. [PMID: 8573077]
2.  Pawelek, J.M. Dopachrome conversion factor functions as an isomerase. Biochem. Biophys. Res. Commun. 166 (1990) 1328–1333. [DOI] [PMID: 2106316]
3.  Pennock, J.L., Behnke, J.M., Bickle, Q.D., Devaney, E., Grencis, R.K., Isaac, R.E. , Joshua. G.W., Selkirk. M.E., Zhang. Y. and Meyer, D.J. Rapid purification and characterization of L-dopachrome-methyl ester tautomerase (macrophage-migration-inhibitory factor) from Trichinella spiralis, Trichuris muris and Brugia pahangi. Biochem. J. 335 (1998) 495–498. [PMID: 9794786]
[EC 5.3.3.12 created 1992, modified 1999, modified 2005]
 
 


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