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Purification and properties of the α‐acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118
Author(s) -
Phalip Vincent,
Monnet Christophe,
Schmitt Philippe,
Renault Pierre,
Godon Jean-Jacques,
Diviès Charles
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00820-5
Subject(s) - lactococcus lactis , valine , isoleucine , biochemistry , leucine , enzyme , allosteric regulation , biology , acetolactate synthase , streptococcaceae , amino acid , chemistry , microbiology and biotechnology , bacteria , genetics , lactic acid , antibiotics
α‐Acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118 was expressed at low levels in cell extracts and was also unstable. The purification was carried out from E. coli in which the enzyme was expressed 36‐fold higher. The specific activity was 24‐fold enhanced after purification. The main characteristics of α‐acetolactate decarboxylase were: (i) activation by the three branched chain amino acids leucine, valine and isoleucine; (ii) allosteric properties displayed in absence and Michaelis kinetics in the presence of leucine. The enzyme is composed of six identical subunits of 26,500 Da.