Abstract
The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29.093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.
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Abbreviations
- ALDC:
-
acetolactate decarboxylase
- CPD-MII:
-
carboxypeptidase II from malt
- CPD-Y:
-
carboxypeptidase Y from yeast
- TFA:
-
trifluoro acetic acid
References
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Svendsen, I., Jensen, B.R. & Ottesen, M. Complete amino acid sequence of α-acetolactate decarboxylase from Bacillus brevis. Carlsberg Res. Commun. 54, 157–163 (1989). https://doi.org/10.1007/BF02907185
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DOI: https://doi.org/10.1007/BF02907185