The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes.
alpha-Lytic protease is a 19.8-kDa protein secreted from the Gram-negative bacterium Lysobacter enzymogenes. We have cloned and sequenced the gene for this serine protease. The nucleotide sequence contains an open reading frame which codes for the 198-residue mature enzyme and a potential prepro-peptide, also of 198 residues. The COOH-terminal 49 residues of the pro-peptide are significantly homologous to the propeptides of Streptomyces griseus proteases A and B. We suggest that this pro-peptide region facilitates formation of the active enzyme. A region bridging the NH2-terminal pre- and pro-peptides is homologous to a maize inhibitor of serine proteases. We speculate that this region inhibits enzymatic activity of the prepro-enzyme.
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases; D001483:Base Sequence; D002918:Chymotrypsin / Q000378:metabolism; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D008969:Molecular Sequence Data; D009710:Nucleotide Mapping; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000032:analysis / Q000235:genetics*; D013302:Streptomyces / Q000201:enzymology
D011480:Protease Inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C021826:myxobacter alpha-lytic proteinase; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases