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Gene Review:

lipA - lipoyl synthase

Pseudomonas protegens Pf-5

McKay, D.B. et al., Aragon, V. et al., Woods, R.G. et al., Beven, C.A. et al., Dieckelmann, M. et al.

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Disease relevance of lipA

AIMS: A lipase-encoding gene (lipA) from a psychrotrophic strain of Pseudomonas fluorescens C9 has previously been characterized [1].

High impact information on lipA

However, loss of lipA and/or lipB did not impair the ability of L. pneumophila to infect Hartmannella amoebae or U937 cell macrophages [2].
Mutations in lipA in particular reduced supernatant activity against mono- and triacylglycerols [2].
The genes encoding protease (aprX) and lipase (lipA) are encoded at opposite ends of a contiguous set of genes which also includes protease inhibitor, Type I secretion functions and two autotransporter proteins [3].
The lipA gene of strain C9 was disrupted by insertional mutagenesis [4].
Southern blot analysis reveals that LS107d2 contains only one esterase and one lipase (encoded by estA and lipA) and this was confirmed by the phenotypes of mutants on triolein and tributyrin-containing agar [5].

References

A strain of Pseudomonas fluorescens with two lipase-encoding genes, one of which possibly encodes cytoplasmic lipolytic activity. Beven, C.A., Dieckelmann, M., Beacham, I.R. J. Appl. Microbiol. (2001) [Pubmed]
Legionella pneumophila genes that encode lipase and phospholipase C activities. Aragon, V., Rossier, O., Cianciotto, N.P. Microbiology (Reading, Engl.) (2002) [Pubmed]
The aprX-lipA operon of Pseudomonas fluorescens B52: a molecular analysis of metalloprotease and lipase production. Woods, R.G., Burger, M., Beven, C.A., Beacham, I.R. Microbiology (Reading, Engl.) (2001) [Pubmed]
The diversity of lipases from psychrotrophic strains of Pseudomonas: a novel lipase from a highly lipolytic strain of Pseudomonas fluorescens. Dieckelmann, M., Johnson, L.A., Beacham, I.R. J. Appl. Microbiol. (1998) [Pubmed]
Degradation of triglycerides by a pseudomonad isolated from milk: the roles of lipase and esterase studied using recombinant strains over-producing, or specifically deficient in these enzymes. McKay, D.B., Dieckelmann, M., Beacham, I.R. J. Appl. Bacteriol. (1995) [Pubmed]

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