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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1984-11

AUTHORS

H. Schütz, F. Radler

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 Km=0.6 mM, glycerol Km=4 mM, ethanediol-1,2 Km=5.3 mM coenzyme B12 (substrate glycerol) Km=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. More... »

PAGES

366-370

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00408381

DOI

http://dx.doi.org/10.1007/bf00408381

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037609294


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