The Isolation and Characterization of a 1,2-Propanediol Oxidoreductase from Neisseria gonorrhoeae

McDonald, Hugh C.; Takeguchi, Milton M.; Detar, Clarence C.; Simon, Paula A.; Livsey, Kim A.; Odstrchel, Gerald; Kaplan, Nathan O.; Weetall, Howard H.

doi:10.1099/00221287-119-2-451

Cited by 4 publications

(5 citation statements)

References 14 publications

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“…Aerobic metabolism of 1,2-propanediol has been described for several species (9,13) and for mutant cells of E. coli (18) able to grow on the diol. In all cases the first step is the oxidation to lactaldehyde through the action of an oxidoreductase.…”

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Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium

et al. 1988

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When grown anaerobically on L-rhamnose, Salmonella typhimurium excreted 1,2-propanediol as a fermentation product. Upon exhaustion of the methyl pentose, 1,2-propanediol was recaptured and further metabolized, provided the culture was kept under anaerobic conditions. n-Propanol and propionate were found in the medium as end products of this process at concentrations one-half that of 1,2-propanediol. As in Klebsiella pneumoniae (T. Toraya, S. Honda, and S. Fukui, J. Bacteriol. 139:3947, 1979), a diol dehydratase which transforms 1,2-propanediol to propionaldehyde and the enzymes involved in a dismutation that converts propionaldehyde to n-propanol and propionate were induced in S. typhimurium cultures able to transform 1,2-propanediol anaerobically.In Escherichia coli, L-rhamnose is metabolized by the sequential action of a rhamnose permease that transports the sugar across the membrane, a rhamnose isomerase (20) that converts it to L-rhamnulose, a rhamnulose kinase (21) that phosphorylates the L-rhamnulose to L-rhamnulose 1-phosphate, and an aldolase (5) that cleaves the L-rhamnulose 1-phosphate into dihydroxyacetone phosphate and L-lactaldehyde. Although no detailed description of the enzymes has been reported, the same pathway has been described in Salmonella typhosa (7) and Salmonella typhimurium (1).Under anaerobic conditions, E. coli induces an NADHdependent oxidoreductase that reduces L-lactaldehyde to 1,2-propanediol, which is excreted into the medium (4). On the basis of propanediol oxidoreductase activity induction and propanediol excretion, this fermentation mechanism has also been proposed for S. typhimurium (3). However, 1,2-propanediol, which is not further metabolized in anaerobic E. coli cultures, gradually disappears from the medium in S. typhimurium cultures maintained under similar anaerobic conditions (J. Badia, unpublished observation).Aerobic metabolism of 1,2-propanediol has been described for several species (9, 13) and for mutant cells of E. coli (18) able to grow on the diol. In all cases the first step is the oxidation to lactaldehyde through the action of an oxidoreductase. Lactaldehyde is subsequently metabolized to lactate and pyruvate (6,17). In contrast, anaerobic metabolism of 1,2-propanediol in Klebsiella pneumoniae (22) or Clostridium glycolicum (8) has been reported to be mediated by a coenzyme B12-dependent diol dehydratase that yields propionaldehyde, which is immediately metabolized by a dismutation to n-propanol and propionate.In this report we characterize the 1,2-propanediol transformation that occurs in S. typhimurium cultures and establish the metabolic pathway involved.

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Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium

et al. 1988

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“…Anti-1,Zpropanediol oxidoreductase serum was prepared in a goat immunized with purified enzyme. The isolation and purification of the enzyme and the preparation of this antiserum are described in detail by McDonald et al (1980). Enzyme inhibition.…”

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“…We have described the isolation and characterization of a gonococcal enzyme which catalyses the conversion of 172-propanediol to an unidentified oxidation product in the presence of NAD+ (McDonald et al, 1980). The possibility of using this enzyme as a diagnostic marker for N. gonorrhoeae prompted us to survey the distribution of the enzyme among various micro-organisms.…”

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The Occurrence of 1,2-Propanediol Oxidoreductase in Micro-organisms and its Use as a Possible Diagnostic Marker for Neisseria gonorrhoeae

et al. 1980

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“…This aminopropanol oxidoreductase catalyzed the oxidation of several vic-diols (such as glycerol, 1,2-propanediol, and 2,3-butanediol) besides D-1-amino-2-propanol (4,14). Since other microbial enzymes are known which catalyze the oxidation of D-1-amino-2-propanol (16,27), glycerol (15,22,24), 1,2-propanediol (11,18), and 2,3-butanediol (26), the question regarding the similarity or differences of these proteins remained unanswered. Glycerol dehydrogenase of E. coli (strain 424) (24) and 1,2-propanediol:NAD+ oxidoreductase of Neisseria gonorrhoeae (18) seemed especially suited for study since both have been purified to homogeneity and several of their properties established.…”

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“…Since other microbial enzymes are known which catalyze the oxidation of D-1-amino-2-propanol (16,27), glycerol (15,22,24), 1,2-propanediol (11,18), and 2,3-butanediol (26), the question regarding the similarity or differences of these proteins remained unanswered. Glycerol dehydrogenase of E. coli (strain 424) (24) and 1,2-propanediol:NAD+ oxidoreductase of Neisseria gonorrhoeae (18) seemed especially suited for study since both have been purified to homogeneity and several of their properties established. This paper presents evidence, both enzymatic and physical, for the identity of the D-1-amino-2-propanol:NAD' oxidoreductase we previously purified and characterized from wild-type E. coli with the glycerol dehydrogenase of E. coli (mutant strain 424) isolated and studied by E. C. C. Lin.…”

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Identity of Escherichia coli D-1-amino-2-propanol:NAD+ oxidoreductase with E. coli glycerol dehydrogenase but not with Neisseria gonorrhoeae 1,2-propanediol:NAD+ oxidoreductase

Kelley¹,

Dekker²

1985

J Bacteriol

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The properties of D-1-amino-2.propanol oxidoreductase from wild-type Escherichia cofi have been compared with those of a glycerol dehydrogenase from mutant E. coli 424 and of a 1,2-propanediol oxidoreductnse from Neisseria gonorrhoeae. Several independent lines of evidence indicate that the former two enzymes are identical. (i) Both enzymatic activities purified to virtual homogeneity in an identical manner, and the ratio of specific activities (glycerol/aminopropanol) remained constant at all stages. (ii) When electrophoresed, both purified enzymes showed a major as well as a minor band of protein coincident with activity, and these two bands from each enzyme had the same mobility. (iii) The subunit molecular weights and isoelectric points were identical for each enzyme, and (iv) kinetic constants (Km and V.1x values) determined wtih three different substrates were the same. The somewhat greater stability of the glycerol dehydrogenase to controlled heat denaturation at 74°C was the only difference observed between these two enzymes. In contrast, D-1-amino-2propanol oxidoreductase was found to be immunochemically and kinetically distinct from the 1,2-propanediol oxidoreductase from N. gonorrhoeae. We have been attempting to uncover and characterize the enzymes that participate in the conversion of L-threonine to the D-1-amino-2-propanol moiety of vitamin B12 (1-5, 14). In earlier studies (3, 5), we demonstrated that enzyme preparations from wild-type Escherichia coli K-12 catalyzed the stepwise conversion of L-threonine-aminoacetone-D-1-amino-2-propanol. Subsequently, we succeeded in purifying L-threonine dehydrogenase (the first required enzyme) to homogeneity from extracts of a mutant of E. coli (1, 2) and, thereafter, also obtained one molecular form of a

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The Isolation and Characterization of a 1,2-Propanediol Oxidoreductase from Neisseria gonorrhoeae

Cited by 4 publications

References 14 publications

Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium

Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium

The Occurrence of 1,2-Propanediol Oxidoreductase in Micro-organisms and its Use as a Possible Diagnostic Marker for Neisseria gonorrhoeae

Identity of Escherichia coli D-1-amino-2-propanol:NAD+ oxidoreductase with E. coli glycerol dehydrogenase but not with Neisseria gonorrhoeae 1,2-propanediol:NAD+ oxidoreductase

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