Isolation, Characterization, and Physiological Role of the Pyruvate Dehydrogenase Complex and Alpha-acetolactate Synthase of Lactococcus Lactis Subsp. Lactis Bv. Diacetylactis

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1992 Jul 1

PMID 1624471

Citations 41

Authors

J L Snoep

M J Teixeira de Mattos

M J Starrenburg

J Hugenholtz

Affiliations

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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.

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