Cited by 26Amino Acid Enzymes and MetabolismEnzyme Production and CharacterizationMicrobial metabolism and enzyme function

Properties of Alanine Dehydrogenase and Aspartase from Propionibacterium freudenreichii subsp. shermanii

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Crow, Vaughan L.·1987·Applied and Environmental Microbiology

Abstract

During lactate fermentation by Propionibacterium freudenreichii subsp. shermanii ATCC 9614, the only amino acid metabolized was aspartate. After lactate exhaustion, alanine was one of the two amino acids to be metabolized. For every 3 mol of alanine metabolized, 2 mol of propionate, 1 mol each of acetate and CO(2), and 3 mol of ammonia were formed. The specific activity of alanine dehydrogenase was 0.08 U/mg of protein during lactate fermentation, and it increased to 0.9 U/mg of protein after lactate exhaustion. Alanine dehydrogenase and aspartase, key enzymes in the metabolism of alanine and aspartate, respectively, were partially purified, and some of their properties were studied. Alanine dehydrogenase had a pH optimum of 9.2 to 9.6 and high K(m) values for both NAD (1 to 4 mM) and alanine (7 to 20 mM). Activity was inhibited by low concentrations of pyruvate and NADH. The pH optimum of aspartase decreased from approximately 7.5 to approximately 6.4 when the MgCl(2) and aspartate concentrations were decreased. Plots of aspartate concentration versus activity showed either hyperbolic or sigmoidal kinetics (interaction coefficient, up to a value of 3.1), depending on pH and MgCl(2) concentration. MgCl(2) was either an activator or an inhibitor, depending on pH and its concentration. Aspartase activity was inhibited by low concentrations of fumarate. The properties of alanine dehydrogenase and aspartase are consistent with the finding that aspartate is metabolized during lact…

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Crossref · 10.1128/aem.53.8.1885-1892.1987

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Authors
Crow, V. L.
Affiliations
New Zealand Dairy Research Institute, Palmerston North, New Zealand
Corresponding author
Crow, Vaughan L.
Venue
Applied and Environmental Microbiology
Published
1987-08
Volume
53
Issue
8
Pages
1885-1892
ISSN
  • 0099-2240 (ISSN-L)
  • 1098-5336
OpenAlex
W1553175189
Cited by
26
References
0
Citations by year
2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2016: 1 · 2014: 1 · 2012: 1
FWCI
0.65
Type
journal article
Language
en
Open access
Locations
  • Applied and Environmental Microbiology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Keywords
alanine dehydrogenase, aspartase, Propionibacterium freudenreichii subsp. shermanii, lactic acid fermentation, aspartate metabolism, alanine metabolism, enzyme kinetics, enzyme inhibition, magnesium chloride, NAD+, pyruvate, fumarate, propionate production, ammonia synthesis

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