3-metil-2-oksobutanoat dehidrogenaza (feredoksin)

3-metil-2-oksobutanoat dehidrogenaza (feredoksin)
Identifikatori
EC broj	1.2.7.7
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

3-metil-2-oksobutanoat dehidrogenaza (feredoksin) (EC 1.2.7.7, 2-ketoizovalerat feredoksinska reduktaza, 3-metil-2-oksobutanoatna sintaza (feredoksin), VOR, reduktaza ketokiselinskog feredoksina razgranatog lanca, reduktaza oksokiselinskog feredoksin razgranatog lanva, keto-valin-feredoksin oksidoreduktaza, ketoizovalerat feredoksinska reduktaza, 2-oksoizovalerat feredoksinska reduktaza) je enzim sa sistematskim imenom 3-metil-2-oksobutanoat:feredoksin oksidoreduktaza (dekarboksilacija; KoA-2-metilpropanoilacija).^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

3-metil-2-oksobutanoat + KoA + 2 oksidovani feredoksin

\rightleftharpoons

S-(2-metilpropanoil)-KoA + CO₂ + 2 redukovani feredoksin + H⁺

Ovaj enzim je jedan od četiri 2-oksokiselinske oksidoreduktaze koji se razlikuju po njihovoj sposobnosti da oksidativno dekarboksilišu različite 2-oksokiseline i formiraju KoA derivate, cf. EC 1.2.7.1, piruvat sintaza; EC 1.2.7.3, 2-oksoglutarat sintaza i EC 1.2.7.8, indolpiruvat feredoksin oksidoreduktaza). Ovaj enzim je KoA-zavistan i sadrži tiamin difosfat u gvožđe-sumporne klastere. On preferentno koristi 2-okso-kiselinske derivate aminokiselina razgranatog lanca, e.g. 3-metil-2-oksopentanoat, 4-metil-2-okso-pentanoat, 2-oksobutirat i 3-metiltiopropanamin.

Reference

↑ Heider, J., Mai, X.H. and Adams, M.W.W. (1996). „Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea”. J. Bacteriol. 178: 780-787. PMID 8550513.
↑ Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. (1997). „Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum”. Eur. J. Biochem. 244: 862-868. PMID 9108258.
↑ Schut, G.J., Menon, A.L. and Adams, M.W.W. (2001). „2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis”. Methods Enzymol. 331: 144-158. PMID 11265457.

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.

Spoljašnje veze

MeSH 3-methyl-2-oxobutanoate+dehydrogenase+(ferredoxin)

[1] Heider, J., Mai, X.H. and Adams, M.W.W. (1996). „Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea”. J. Bacteriol. 178: 780-787. PMID 8550513.

[2] Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. (1997). „Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum”. Eur. J. Biochem. 244: 862-868. PMID 9108258.

[3] Schut, G.J., Menon, A.L. and Adams, M.W.W. (2001). „2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis”. Methods Enzymol. 331: 144-158. PMID 11265457.

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