1arc
From Proteopedia
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THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE
Overview
The complete amino acid sequence of Achromobacter lyticus protease I (EC, 3.4.21.50), which specifically hydrolyzes lysyl peptide bonds, has been, established. This has been achieved by sequence analysis of the reduced, and S-carboxymethylated protease and of peptides obtained by enzymatic, digestion with Achromobacter protease I itself and Staphylococcus aureus, V8 protease and by chemical cleavage with cyanogen bromide. The protease, consists of 268 residues with three disulfide bonds, which have been, assigned to Cys6-Cys216, Cys12-Cys80, and Cys36-Cys58. Comparison of the, amino acid sequence of Achromobacter protease and other serine proteases, of bacterial and mammalian origins has revealed that Achromobacter, protease I is a mammalian-type serine protease of which the catalytic, triad comprises His57, Asp113, and Ser194. It has also been shown that the, protease has 9- and 26-residue extensions of the peptide chain at the N, and C termini, respectively, and overall sequence homology is as low as, 20% with bovine trypsin. The presence of a disulfide bridge between the, N-terminal extension Cys6 and Cys216 close to the putative active site in, the C-terminal region is thought to be responsible for the generation of, maximal proteolytic function in the pH range 8.5-10.7 and enhanced, stability to denaturation.
About this Structure
1ARC is a Single protein structure of sequence from Achromobacter lyticus with TCK as ligand. Active as Lysyl endopeptidase, with EC number 3.4.21.50 Full crystallographic information is available from OCA.
Reference
The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease., Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F, J Biol Chem. 1989 Mar 5;264(7):3832-9. PMID:2492988
Page seeded by OCA on Tue Nov 20 11:04:10 2007
