title: Identification and characterization of an autolysin gene, atlA, from Streptococcus criceti.
abstract: AtlA of Streptococcus mutans is a major autolysin and belongs to glycoside hydrolase family 25 with cellosyl of Streptomyces coelicolor. The autolysin gene (atlA) encoding AtlA was identified from S. criceti. AtlA of S. criceti comprises the signal sequence in the N-terminus, the putative cell-wall-binding domain in the middle, and the catalytic domain in the C-terminus. Homology modeling analysis of the catalytic domain of AtlA showed the resemblance of the spatial arrangement of five amino acids around the predicted catalytic cavity to that of cellosyl. Recombinant AtlA and its four point mutants, D655A, D747A, W831A, and D849A, were evaluated on zymogram of S. criceti cells. Lytic activity was destroyed in the mutants D655A and D747A and diminished in the mutants W831A and D849A. These results suggest that Asp655 and Asp747 residues are critical for lytic activity and Trp831 and Asp849 residues are also associated with enzymatic activity.
authors.affiliation: Division of Bioregulatory Pharmacology, Department of Pharmacology, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba-cho 028-3694, Japan. htamura@iwate-med.ac.jp
authors.forename: Haruki
authors.initials: H
authors.lastname: Tamura
authors.forename: Arisa
authors.initials: A
authors.lastname: Yamada
authors.forename: Hirohisa
authors.initials: H
authors.lastname: Kato
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D013291:Streptococcus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D009238:N-Acetylmuramoyl-L-alanine Amidase