A lipase of Aeromonas hydrophila showing nonhemolytic phospholipase C activity

Ingham A.B. and Pemberton J.M. (1995) A lipase of Aeromonas hydrophila showing nonhemolytic phospholipase C activity. Current Microbiology, 31 1: 28-33. doi:10.1007/BF00294630

Author Ingham A.B.
Pemberton J.M.
Title A lipase of Aeromonas hydrophila showing nonhemolytic phospholipase C activity
Journal name Current Microbiology   Check publisher's open access policy
ISSN 0343-8651
Publication date 1995-01-01
Sub-type Article (original research)
DOI 10.1007/BF00294630
Volume 31
Issue 1
Start page 28
End page 33
Total pages 6
Publisher Springer-Verlag
Subject 2404 Microbiology
Abstract Extracellular lipase activity detected on tributyrin agar has been identified in a cosmid clone, JMP3084, constructed from the chromosome of Aeromonas hydrophila and vector pHC79. This lipase, named apl-1, also exhibits nonhemolytic phospholipase C activity on lecithin and p-nitrophenylphosphorylcholine. Subcloning of the cosmid JMP3084 with partial Sau3a1 digestion localized the lipase gene to a 3.4-kb DNA fragment. Southern blot analysis shows the gene apl-1 to exist in single copy on the A. hydrophila chromosome. Expression of apl-1 in the pT7 system identified a single protein of molecular weight 70 kDa. Nucleotide sequencing of apl-1 has identified an open reading frame of 2055 bases predicting a protein of 73 kDa. The presence of an amino terminal signal sequence of 18 amino acids accounts for this molecular weight disparity. Further analysis of the lipase amino acid sequence revealed the presence of a classical serine active lipase site (Gly-X-Ser-X-Gly) located between residues 561 and 570. The A. hydrophila chromosomal copy of apl-1 has been inactivated by use of the mutagenesis vector pJP5603, resulting in the complete removal of phospholipase C activity and lowered levels of lipase activity detected on tributyrin agar.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
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Citation counts: TR Web of Science Citation Count  Cited 12 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 16 times in Scopus Article | Citations
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