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PMID: 1624471 Published · ppublish English Journal Article

Isolation, characterization, and physiological role of the pyruvate dehydrogenase complex and alpha-acetolactate synthase of Lactococcus lactis subsp. lactis bv. diacetylactis.

Journal of bacteriology ·Vol. 174 ·No. 14 ·1992-07-00 ·Pages 4838-41

Snoep JL, Teixeira de Mattos MJ, Starrenburg MJ, Hugenholtz J

Abstract

The pyruvate dehydrogenase complex of Lactococcus lactis subsp. lactis bv. diacetylactis has a specific activity of 6.6 U/mg and a Km of 1 mM for pyruvate. The specific activities of E2 and E3 in the complex are 30 and 0.36 U/mg, respectively. The complex is very sensitive to NADH inhibition and consists of four subunits: E1 alpha (44 kDa), E1 beta (35 kDa), E2 (73 kDa), and E3 (60 kDa). The L. lactis alpha-acetolactate synthase has a specific activity of 103 U/mg and a Km of 50 mM for pyruvate. Thiamine pyrophosphate (Km = 3.2 microM) and divalent cations are essential for activity. The native enzyme measures 172 kDa and consists of 62-kDa monomers. The role of both enzymes in product formation is discussed in view of NADH inhibition and competition for pyruvate.

MeSH Terms
Acetolactate Synthase/isolation & purification,metabolism Cations, Divalent/metabolism Chromatography, High Pressure Liquid Kinetics Lactococcus lactis/enzymology NAD/metabolism Pyruvate Dehydrogenase Complex/isolation & purification,metabolism Pyruvates/metabolism Pyruvic Acid Thiamine Pyrophosphate/metabolism
Chemicals
Cations, Divalent Pyruvate Dehydrogenase Complex Pyruvates NAD Pyruvic Acid Acetolactate Synthase Thiamine Pyrophosphate
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Snoep J L
Department of Microbiology, University of Amsterdam, The Netherlands.
Teixeira de Mattos M J
Starrenburg M J
Hugenholtz J
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.174.14.4838-4841.1992
Published
1992-07-00
Pages
4838-41
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC206284
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.174.14.4838-4841.1992 PMC Full Text View journal details
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