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Fosfonoacetaldehid reduktaza (NADH)
Fosfonoacetaldehid reduktaza (NADH)
Identifikatori
EC broj	1.1.1.309
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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Fosfonoacetaldehid reduktaza (NADH) (EC 1.1.1.309, PhpC) je enzim sa sistematskim imenom 2-hidroksietilfosfonat:NAD⁺ oksidoreduktaza.^[1] Ovaj enzim katalizuje sledeću hemijsku reakciju

2-hidroksietilfosfonat + NAD⁺

\rightleftharpoons

fosfonoacetaldehid + NADH + H⁺

Ovaj enzim iz Streptomyces viridochromogenes katalizuje korak u biosintezi fosfinotricin tripeptida, redukciju fosfonoacetaldehida do 2-hidroksietilfosfonata. Preferirani kofaktor je NADH. Enzim je u manjoj meri aktivan sa NADPH.

Reference

^ Blodgett, J.A., Thomas, P.M., Li, G., Velasquez, J.E., van der Donk, W.A., Kelleher, N.L. and Metcalf, W.W. (2007). „Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide”. Nat. Chem. Biol. 3: 480—485. PMID 17632514.

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

Phosphonoacetaldehyde+reductase+(NADH) на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Blodgett, J.A., Thomas, P.M., Li, G., Velasquez, J.E., van der Donk, W.A., Kelleher, N.L. and Metcalf, W.W. (2007). „Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide”. Nat. Chem. Biol. 3: 480—485. PMID 17632514.

[1]