1ARB

THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE

Summary for 1ARB

• Entry DOI: 10.2210/pdb1arb/pdb
• Descriptor: ACHROMOBACTER PROTEASE I (2 entities in total)
• Functional Keywords: hydrolase(serine protease)
• Biological source: Achromobacter lyticus
• Cellular location: Secreted: P15636
• Total number of polymer chains: 1
• Total formula weight: 27759.23

Authors

Kitagawa, Y.,Katsube, Y. (deposition date: 1993-04-15, release date: 1993-10-31, Last modification date: 2024-06-05)

Primary citation

Tsunasawa, S.,Masaki, T.,Hirose, M.,Soejima, M.,Sakiyama, F.
The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease.
J.Biol.Chem., 264:3832-3839, 1989

PubMed Abstract: 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.

PubMed: 2492988

Experimental method

X-RAY DIFFRACTION (1.2 Å)