Cloning of a Lysobacter enzymogenes gene that encodes an arginyl endopeptidase (endoproteinase Arg-C)

• Published in: Biochimica et biophysica acta Vol. 1443; no. 3; pp. 369 - 374
• Main Authors: Wright, Denis S., Graham, Lloyd D., Jennings, Philip A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 22-12-1998
• Subjects: Amino Acid Sequence; Arginyl endopeptidase; Base Sequence; Cloning, Molecular; DNA, Bacterial - chemistry; DNA, Bacterial - genetics; Electrophoresis, Polyacrylamide Gel; Endoproteinase Arg-C; Genes, Bacterial - genetics; Gram-Negative Bacteria - chemistry; Gram-Negative Bacteria - enzymology; Gram-Negative Bacteria - genetics; Lysobacter; Molecular Sequence Data; Open Reading Frames; Promoter Regions, Genetic; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; Serine protease; Substrate Specificity; Subtilase; Subtilisin; Endoproteinase Arg-C; Serine protease; Subtilisin; Arginyl endopeptidase; Subtilase; Lysobacter
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/S0167-4781(98)00228-0

Screening an expression library of
Lysobacter enzymogenes DNA allowed us to clone a gene encoding a serine protease that cleaves synthetic substrates C-terminal to Arg and, to a lesser extent, Lys residues. The gene product, which shares sequence homology with the lysyl endopeptidases from
L. enzymogenes and
Achromobacter lyticus, consists of a signal sequence (24 residues), pro-region (∼195 residues), and catalytic domain (∼244 residues). Downstream of this gene is an open reading frame that lacks a promoter and appears to encode an inactive type I subtilase.