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Propanediol-1,2-dehydratase and metabolism of glycerol of Lactobacillus brevis

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Abstract

While most strains of heterofermentative lactobacilli and strains of Leuconostoc species contained only traces of a dehydratase reacting with glycerol or propanediol-1,2, three strains of Lactobacillus brevis and one strain of L. buchneri that metabolized glycerol readily in the presence of glucose, contained propanediol-1,2 dehydratase (EC 4.2.1.28). This cobamide requiring enzyme from L. brevis B 18 was partially purified. It reacts with the substrates propanediol-1,2, glycerol and ethanediol-1,2 with the relative activities of about 3:2:1. This ratio remained unchanged throughout the purification procedure. The substrate affinities were measured: propanediol-1,2 K m=0.6 mM, glycerol K m=4 mM, ethanediol-1,2 K m=5.3 mM coenzyme B12 (substrate glycerol) K m=0.007 mM. The activity of the dehydratase was promoted by potassium or ammonium ions and inhibited by sodium, lithium, magnesium or specially manganese. The apparent molecular weight of propanediol-1,2 dehydratase was determined as Mr=180,000.

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Correspondence to F. Radler.

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Dedicated to Prof. Dr. H. G. Schlegel on behalf of his 60th birthday

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Schütz, H., Radler, F. Propanediol-1,2-dehydratase and metabolism of glycerol of Lactobacillus brevis . Arch. Microbiol. 139, 366–370 (1984). https://doi.org/10.1007/BF00408381

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Key words

  • Lactic acid bacteria
  • Lactobacillus brevis
  • Propanediol-1,2-dehydratase
  • Propanediol-1,2
  • Glycerol
  • Ethanediol-1,2