title: Complete amino acid sequence of alpha-acetolactate decarboxylase from Bacillus brevis.
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.
authors.affiliation: Carlsberg Laboratory, Department of Chemistry, Copenhagen Valby.
authors.forename: I
authors.initials: I
authors.lastname: Svendsen
authors.forename: B R
authors.initials: BR
authors.lastname: Jensen
authors.forename: M
authors.initials: M
authors.lastname: Ottesen
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000201:enzymology*; D002262:Carboxy-Lyases; D003488:Cyanogen Bromide; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D012697:Serine Endopeptidases; D014357:Trypsin
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin; D002262:Carboxy-Lyases; C023746:acetolactate decarboxylase; D003488:Cyanogen Bromide