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GDP-L-fukoza sintaza
Identifikatori
EC broj	1.1.1.271
CAS broj	113756-18-6
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

GDP-L-fukoza sintaza (EC 1.1.1.271, GDP-4-keto-6-dezoksi-D-manoza-3,5-epimerase-4-reduktaza, GDP-L-fukoza:NADP⁺ 4-oksidoreduktaza (3,5-epimerizacija)) je enzim sa sistematskim imenom GDP-beta-L-fukoza:NADP+ 4-oksidoreduktaza (3,5-epimerizacija).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

GDP-beta-L-fukoza + NADP⁺

\rightleftharpoons

GDP-4-dehidro-6-dezoksi-alfa-D-manoza + NADPH + H⁺

Enzimi čoveka i Escherichia coli koriste NADH umesto NADPH u izvesnoj meri.

Reference

↑ Chang, S., Duerr, B. and Serif, G. (1988). „An epimerase-reductase in L-fucose synthesis”. J. Biol. Chem. 263: 1693-1697. PMID 3338988.
↑ Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. (2000). „Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae”. Glycobiology 10: 1041-1047. PMID 11030750.
↑ Menon, S., Stahl, M., Kumar, R., Xu, G.-Y. and Sullivan, F. (1999). „Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli”. J. Biol. Chem. 274: 26743-26750. PMID 10480878.
↑ Somers, W.S., Stahl, M.L. and Sullivan, F.X. (1998). „GDP-fucose synthetase from Escherichia coli: Structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site”. Structure 6: 1601-1612. PMID 9862812.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH GDP-L-fucose+synthase

[1] Chang, S., Duerr, B. and Serif, G. (1988). „An epimerase-reductase in L-fucose synthesis”. J. Biol. Chem. 263: 1693-1697. PMID 3338988.

[2] Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. (2000). „Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae”. Glycobiology 10: 1041-1047. PMID 11030750.

[3] Menon, S., Stahl, M., Kumar, R., Xu, G.-Y. and Sullivan, F. (1999). „Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli”. J. Biol. Chem. 274: 26743-26750. PMID 10480878.

[4] Somers, W.S., Stahl, M.L. and Sullivan, F.X. (1998). „GDP-fucose synthetase from Escherichia coli: Structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site”. Structure 6: 1601-1612. PMID 9862812.

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