The Journal of Biochemistry · 1999 · 22 citations · 0 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProtein TranslationEnzyme CharacterizationProtein Sequence AnalysisProteolytic EnzymesBacterial ProteasesMicrobial ProteasesMolecular Weight DeterminationNucleotide Sequence SearchPeptidase Activity
We deduced the amino acid sequence of Escherichia coli lysophospholipase L(1) by determining the nucleotide sequence of the pldC gene encoding this enzyme. The translated protein was found to contain 208 amino acid residues with a hydrophobic leader sequence of 26 amino acid residues. The molecular weight of the purified enzyme (20,500) was in good agreement with the predicted size (20,399) of the processed protein. A search involving a data bank showed that the nucleotide sequence of the pldC gene was identical to those of the apeA and tesA genes encoding protease I and thioesterase I, respectively. Consistent with the identity of the pldC gene with these two genes, the enzyme purified from E. coli overexpressing the pldC gene showed both protease I and thioesterase I activities.