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Metilmalonat-semialdehid dehidrogenaza (acilacija)
	Tetramer metilmalonat-semialdehid dehidrogenaze (Bacillus subtilis)
Identifikatori
EC broj	1.2.1.27
CAS broj	37205-49-5
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

Metilmalonat-semialdehid dehidrogenaza (acilacija) (EC 1.2.1.27, MSDH, MMSA dehidrogenaza) je enzim sa sistematskim imenom 2-metil-3-oksopropanoat:NAD⁺ 3-oksidoreduktaza (KoA-propanoilacija).^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

2-metil-3-oksopropanoat + KoA +H₂O + NAD⁺

\rightleftharpoons

propanoil-KoA + HCO₃^- + NADH

Ovaj enzim takođe konvertuje 3-oksopropanoat u acetil-KoA. Reakcija se odvija u dva koraka, pri čemu dekarboksilacioni process teče uz KoA vezivanje. Bikarbonat umesto CO² se oslobađa kao finalni produkt.

Reference

↑ Sokatch, J.R., Sanders, L.E. and Marshall, V.P. (1968). „Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine”. J. Biol. Chem. 243: 2500-2506. PMID 4297649.
↑ Dubourg, H., Stines-Chaumeil, C., Didierjean, C., Talfournier, F., Rahuel-Clermont, S., Branlant, G. and Aubry, A. (2004). „Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis”. Acta Crystallogr. D Biol. Crystallogr. 60: 1435-1437. PMID 15272169.
↑ Stines-Chaumeil, C., Talfournier, F. and Branlant, G. (2006). „Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis”. Biochem. J. 395: 107-115. PMID 16332250.

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 Methylmalonate-semialdehyde+dehydrogenase+(acylating)

[1] Sokatch, J.R., Sanders, L.E. and Marshall, V.P. (1968). „Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine”. J. Biol. Chem. 243: 2500-2506. PMID 4297649.

[2] Dubourg, H., Stines-Chaumeil, C., Didierjean, C., Talfournier, F., Rahuel-Clermont, S., Branlant, G. and Aubry, A. (2004). „Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis”. Acta Crystallogr. D Biol. Crystallogr. 60: 1435-1437. PMID 15272169.

[3] Stines-Chaumeil, C., Talfournier, F. and Branlant, G. (2006). „Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis”. Biochem. J. 395: 107-115. PMID 16332250.

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