Histidine decarboxylase of Lactobacillus 30a. Sequences of the cyanogen bromide peptides from the alpha chain.
The alpha chain of histidine decarboxylase contains eight internal methionine residues. After reductive amination to convert the NH2-terminal pyruvoyl residue to an alanyl residue and cyanogen bromide treatment, 13 pure peptides were isolated. Four of these are incomplete cleavage products. The sequence of each of the remaining nine peptides was established by automated and manual degradation of the intact peptides and of smaller peptides obtained from tryptic, chymotryptic, and staphylococcal protease digests of the cyanogen bromide peptides. These results, together with the data on overlapping peptides reported in the accompanying paper (Huynh, Q. K., Recsei, P. A., Vaaler, G. L., and Snell, E. E. (1984) J. Biol. Chem. 259, 2833-2839), establish the complete amino acid sequence of the alpha chain.
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000302:isolation & purification; D003488:Cyanogen Bromide; D006640:Histidine Decarboxylase / Q000302:isolation & purification; D007778:Lactobacillus / Q000201:enzymology*; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis
D046911:Macromolecular Substances; D010446:Peptide Fragments; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase; D003488:Cyanogen Bromide