title: [Primary structure of histidine decarboxylase].
abstract: The results of investigation of the primary structure of the Histidine Decarboxylase Micrococcus sp. n. are reported. A comparison of the primary structure of the Histidine Decarboxylase Micrococcus sp. n. with that of the Lactobacillus 30a enzyme suggests the alignment with a 52% identity. It is therefore highly probable that two proteins have evolved from common ancestry. The conservative amino acid sequences with residues (pyruvate, cysteine) of the active center have been found.
authors.forename: V N
authors.initials: VN
authors.lastname: Prozorovskiĭ
authors.forename: A E
authors.initials: AE
authors.lastname: Alekseeva
authors.forename: O G
authors.initials: OG
authors.lastname: Grebenshchikova
mesh_terms: D000595:Amino Acid Sequence; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase; D007778:Lactobacillus / Q000201:enzymology; D008837:Micrococcus / Q000201:enzymology; D008969:Molecular Sequence Data
chemical_list: D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase
vernacular_title: Pervichnaia struktura gistidindekarboksilazy.