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. 1973 May;134(1):167–182. doi: 10.1042/bj1340167

Microbial metabolism of amino alcohols. 1-Aminopropan-2-ol and ethanolamine metabolism via propionaldehyde and acetaldehyde in a species of Pseudomonas

A Jones 1,*, J M Turner 1
PMCID: PMC1177797  PMID: 4723219

Abstract

1. Growth and manometric experiments showed that a Pseudomonas sp. P6 (N.C.I.B. 10431), formerly known as Achromobacter sp. P6, was capable of growth on both stereoisomers of 1-aminopropan-2-ol, and supported the hypothesis that assimilation involved metabolism to propionaldehyde, propionate and possibly 2-hydroxyglutarate. A number of alternative intermediary metabolites were ruled out. 2. Accumulation of propionaldehyde from 1-aminopropan-2-ol by intact cells occurred only during active growth, was transitory and was accompanied by morphological changes in the pseudomonad. 3. Enzymic and radioactive tracer evidence showed that 1-aminopropan-2-ol O-phosphate was the intermediate between amino alcohol and aldehyde. The operation of an inducibly formed ATP–amino alcohol phosphotransferase was established by measuring substrate disappearance, ADP formation and amino alcohol O-phosphate formation. This novel kinase had two activity peaks at about pH7 and 9. It acted on both l- and d-isomers of 1-aminopropan-2-ol, and also on l-threonine and ethanolamine, but had only low activity towards choline. The enzyme was partially purified by ion-exchange chromatography. 4. An amino alcohol O-phosphate phospho-lyase (deaminating) produced propionaldehyde from dl- and d-1-aminopropan-2-ol O-phosphate, and also formed acetaldehyde less rapidly from ethanolamine O-phosphate. It had optimum activity at about pH8 in Tris–HCl buffers. The enzyme was partially purified and evidence was obtained that a single enzyme was responsible for both activities. Apparent Km values for the substrates were determined. Activity was inhibited by dl-threonine O-phosphate, dl-serine O-phosphate, choline O-phosphate and Pi. Enzyme formation was induced by growth with either amino alcohol substrate. 5. Radioactive tracer experiments with dl-1-amino[3-14C]propan-2-ol confirmed the operation of the amino alcohol kinase and demonstrated coupling with the phospho-lyase enzyme in vitro to produce [14C]-propionaldehyde. 6. An aldehyde dehydrogenase, found in extracts of the pseudomonad after growth on 1-aminopropan-2-ol, was characterized and concluded to be responsible for propionaldehyde and acetaldehyde oxidation. The enzyme was inactive with methylglyoxal. 7. Propionate and acetate were concluded to be metabolized via propionyl-CoA and acetyl-CoA, and studies were made of a CoA ester synthase found in extracts. 8. Studies of a strain of Pseudomonas putida N.C.I.B. 10558 suggested that 1-aminopropan-2-ols were metabolized via their O-phosphates, propionaldehyde and propionate. Amino alcohol kinase activity was detected and extracts contained a phospho-lyase showing higher activity with the 1-aminopropan-2-ol O-phosphate than with ethanolamine O-phosphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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