(R)-aminopropanol dehydrogenase

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In enzymology, a (R)-aminopropanol dehydrogenase (EC 1.1.1.75) is an enzyme that catalyzes the chemical reaction

(R)-1-aminopropan-2-ol + NAD⁺ $\rightleftharpoons$ aminoacetone + NADH + H⁺

Thus, the two substrates of this enzyme are (R)-1-aminopropan-2-ol and NAD⁺, whereas its 3 products are aminoacetone, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-1-aminopropan-2-ol:NAD+ oxidoreductase. Other names in common use include L-aminopropanol dehydrogenase, 1-aminopropan-2-ol-NAD+ dehydrogenase, L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase, 1-aminopropan-2-ol-dehydrogenase, DL-1-aminopropan-2-ol: NAD+ dehydrogenase, and L(+)-1-aminopropan-2-ol-NAD+/NADP+ oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It requires potassium as a cofactor.

[edit] References

IUBMB entry for 1.1.1.75
BRENDA references for 1.1.1.75 (Recommended.)
PubMed references for 1.1.1.75
PubMed Central references for 1.1.1.75
Google Scholar references for 1.1.1.75
Dekker EE, Swain RR (1968). "Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli". Biochim. Biophys. Acta. 158: 306–7. PMID 4385233.
Tuner JM (1966). "Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrgenase in Escerichia coli". Biochem. J. 99: 427–33. PMID 5329339.
Turner JM (1967). "Microbial metabolism of amino ketones. L-1-aminopropan-2-ol dehydrogenase and L-threonine dehydrogenase in Escherichia coli". Biochem. J. 104: 112–21. PMID 5340733.