Microbial Metabolism of Amino Ketones: D-1-Aminopropan-2-ol and Aminoacetone Metabolism in Escherichia coli

Lowe, David; Turner, D. J. M.

doi:10.1099/00221287-63-1-49

Cited by 18 publications

(11 citation statements)

References 9 publications

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“…gonorrhoeae. Similar enzymes have been reported in a soil pseudomonad (Lowe & Turner, 1968), in E. coli wild-type (Lowe & Turner, 1968, 1970, in E. coli mutants (Sridhara et al, 1969), in anaerobically cultured E. coli (Cocks et al, 1974;Boronat & Aguilar, 1979), and in a soil bacterium isolated by Tanaka et al (1975). Based on substrate specificity, the gonococcal enzyme and the soil bacterium dehydrogenase (Tanaka et al, 1975) were the most similar.…”

Section: Discussionsupporting

confidence: 73%

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

et al. 1980

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An enzyme which oxidizes 1 ,2-propanediol in the presence of NAD+ has been purified from lysates of Neisseria gonorrhoeae. The enzyme was activated by monovalent cations, had a pH optimum between 9 and 10, and showed a substrate specificity unlike any known alcohol or glycerol dehydrogenase. The enzyme had an apparent K, of 17 mM for 7,2-propanediol and 0.37 mM for NADf. When chromatographed on a Sephadex G-150 column, the enzyme eluted as a single peak in the molecular weight region of a bovine serum albumin marker. An antibody to the purified enzyme was prepared in goats. When antiserum was reacted with the enzyme in immunodiffusion experiments, a single precipitin band was detected. When the enzyme was mixed with an excess of antibody and then reacted with substrate, enzyme activity was completely inhibited.

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Section: Discussionsupporting

confidence: 73%

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

et al. 1980

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“…The uncertainty with respect to the physiological function of dihydroxyacetone reductase is not unique to yeasts. Lowe and Turner (1970) purified an enzyme from Escherichia coli which they designated 1-amino-2-propanol dehydrogenase. This enzyme showed the highest activity with dihydroxyacetone and, like the enzyme from H .…”

Section: Discussionmentioning

confidence: 99%

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

Verduyn¹,

Breedveld²,

Schreuder³

et al. 1988

Yeast

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Nunsmulu poljworpha CBS 4732 grown on a variety of substrates contained very high activities of enzymes catalyzing the NADH-linked reduction of dihydroxyacetone, acetoin, diacetyl, acetol, methylglyoxal and acetone. The enzymes catalyzing these reductions have been purified and their kinetic properties are described. Three different enzymes were found responsible for the above-mentioned activities, namely: (1) dihydroxyacetone reductase; (2) acetone reductase; and (3) alcohol dehydrogenase.So far, the physiological function of dihydroxyacetone reductase and acetone reductase is obscure. The kinetic properties of dihydroxyacetone reductase and the regulation of the synthesis of this enzyme suggest that it does not function as a glycerol dehydrogenase.

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“…These enzymes might be involved in the metabolism of aminoacetone, which is formed from threonine in the case of B. subtilis (Willetts and Turner 1971). On the other hand, NAD + -dependent d-1amino-2-propanol dehydrogenase, which is also involved in threonine metabolism via aminoacetone, was found in E. coli cells (Dekker and Swain 1968;Lowe and Turner 1970;Campbell and Dekker 1973;Campbell et al 1978;Dekker 1984, 1985). These enzymes might play important roles in the metabolism of 1-amino-2-propanol, aminoacetone or threonine, but biochemical and enzymological analysis of their enzyme properties has been insufficient, especially for l-1amino-2-propanol dehydrogenase.…”

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confidence: 99%

A novel NADP⁺-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols

Kataoka

Nakamura

Urano

et al. 2006

Lett Appl Microbiol

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Aim: A novel NADP+‐dependent l‐1‐amino‐2‐propanol dehydrogenase was isolated from Rhodococcus erythropolis MAK154, and characterized. Methods and Results: The enzyme was inducibly produced on cultivation with aminoalcohols such as 1‐amino‐2‐propanol, 1‐amino‐2‐butanol and 2‐aminocyclohexanol. The enzyme catalyses the NADP+‐dependent oxidation of several aminoalcohols, and also the NADPH‐dependent asymmetric reduction of an aminoketone compound to a double chiral aminoalcohol, d‐pseudoephedrine. Amino acid sequence analysis showed that the enzyme might belong to the short‐chain dehydrogenase/reductase family. Conclusions: NADP+‐dependent l‐1‐amino‐2‐propanol dehydrogenase isolated from R. erythropolis MAK154 reversibly catalysed dehydrogenation of aminoalcohols, and exhibited a unique sterospecifity for the reduction reaction. Significance and Impact of the Study: The enzyme is a promising catalyst for the production of double chiral compound, d‐pseudoephedrine, from prochiral substrate.

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Microbial Metabolism of Amino Ketones: D-1-Aminopropan-2-ol and Aminoacetone Metabolism in Escherichia coli

Cited by 18 publications

References 9 publications

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

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

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

A novel NADP⁺-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols

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Microbial Metabolism of Amino Ketones: D-1-Aminopropan-2-ol and Aminoacetone Metabolism in Escherichia coli

Cited by 18 publications

References 9 publications

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

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

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

A novel NADP+-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols

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Product

Resources

About

A novel NADP⁺-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols