Biology:(R)-aminopropanol dehydrogenase
| (R)-aminopropanol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.75 | ||||||||
| CAS number | 37250-13-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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+ [math]\displaystyle{ \rightleftharpoons }[/math] 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.
References
- "Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli". Biochim. Biophys. Acta 158 (2): 306–7. 1968. doi:10.1016/0304-4165(68)90150-5. PMID 4385233. https://deepblue.lib.umich.edu/bitstream/2027.42/33173/1/0000559.pdf.
- Tuner JM (1966). "Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in Escherichia coli". Biochem. J. 99 (2): 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 (1): 112–21. PMID 5340733.
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