Molecular analysis and expression of the lipase of Staphylococcus epidermidis.
Lipase of Staphylococcus epidermidis 9 was purified from culture supernatant fluid. Two polypeptides (51 and 43 kDa) were detected by SDS-PAGE, of which the 43 kDa polypeptide reacted with anti-lipase serum. The S. epidermidis 9 lipase gene (gehC) was cloned in Escherichia coli and localized to a 2.1 kb sequence by subcloning and transposon mutagenesis. The nucleotide sequence of gehC (2064 nucleotides) was determined and the predicted amino acid sequence of the encoded lipase (77 kDa) identified. A 97 kDa lipase was detected in extracts of E. coli harbouring gehC and in post-exponential-phase culture supernatant fluids of S. epidermidis 9. Data presented indicate that the lipase behaves anomalously during SDS-PAGE and that a pro-lipase is proteolytically processed in cultures of S. epidermidis 9 during growth.
Farrell
A M
AM
Department of Microbiology, University of Leeds, UK.
Foster
T J
TJ
Holland
K T
KT
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003470:Culture Media; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005798:Genes, Bacterial; D008049:Lipase / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013210:Staphylococcus / Q000201:enzymology / Q000235:genetics; D013212:Staphylococcus epidermidis / Q000201:enzymology* / Q000235:genetics
D003470:Culture Media; D008049:Lipase