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D-dopahromna dekarboksilaza
D-dopahromna dekarboksilaza
Identifikatori
EC broj	4.1.1.84
CAS broj	184111-06-6
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
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NCBI	proteini

D-dopahromna dekarboksilaza (EC 4.1.1.84, fenilpiruvatna tautomeraza II, D-tautomeraza, D-dopahromna tautomeraza, D-dopahromna karboksilijaza) je enzim sa sistematskim imenom D-dopachrome karboksilijaza (formira 5,6-dihidroksiindol).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

D-dopahrom

\rightleftharpoons

5,6-dihidroksiindol + CO₂

Ovaj enzim je specifičan za D-dopahrom kao supstrat.

Reference

^ Odh, G., Hindemith, A., Rosengren, A.M., Rosengren, E. and Rorsman, H. (1993). „Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole”. Biochem. Biophys. Res. Commun. 197: 619—624. PMID 8267597.
^ Yoshida, H., Nishihira, J., Suzuki, M. and Hikichi, K. (1997). „NMR characterization of physicochemical properties of rat D-dopachrome tautomerase”. Biochem. Mol. Biol. Int. 42: 891—899. PMID 9285056.
^ Sugimoto, H., Taniguchi, M., Nakagawa, A., Tanaka, I., Suzuki, M. and Nishihira, J. (1999). „Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 Å resolution”. Biochemistry. 38: 3268—3279. PMID 10079069.
^ Nishihira, J., Fujinaga, M., Kuriyama, T., Suzuki, M., Sugimoto, H., Nakagawa, A., Tanaka, I. and Sakai, M. (1998). „Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation”. Biochem. Biophys. Res. Commun. 243: 538—544. PMID 9480844.

Literatura

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

D-dopachrome+decarboxylase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Odh, G., Hindemith, A., Rosengren, A.M., Rosengren, E. and Rorsman, H. (1993). „Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole”. Biochem. Biophys. Res. Commun. 197: 619—624. PMID 8267597.

[2] Yoshida, H., Nishihira, J., Suzuki, M. and Hikichi, K. (1997). „NMR characterization of physicochemical properties of rat D-dopachrome tautomerase”. Biochem. Mol. Biol. Int. 42: 891—899. PMID 9285056.

[3] Sugimoto, H., Taniguchi, M., Nakagawa, A., Tanaka, I., Suzuki, M. and Nishihira, J. (1999). „Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 Å resolution”. Biochemistry. 38: 3268—3279. PMID 10079069.

[4] Nishihira, J., Fujinaga, M., Kuriyama, T., Suzuki, M., Sugimoto, H., Nakagawa, A., Tanaka, I. and Sakai, M. (1998). „Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation”. Biochem. Biophys. Res. Commun. 243: 538—544. PMID 9480844.

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