Disease relevance of PFL_0617

• Serratia marcescens ATP-binding cassette (ABC) exporter, the Lip system, secretes lipase (LipA(SM)), metalloproteases, and a cell surface layer protein homologue but not a heme acquisition protein, HasA (HasA(SM)) [1].
• The Pseudomonas fluorescens lipase has a C-terminal secretion signal and is secreted by a three-component bacterial ABC-exporter system [2].
• In Escherichia coli, the three proteins AprD, AprE, AprF are necessary and sufficient for efficient secretion of lipase to the extracellular medium [2].
• Formation of orange-red fluorescent plaques on rhodamine B-triolein plates was used to identify phages carrying the lipase gene [3].
• A threading model of PhaC1Po, developed based on homology of the enzyme to the Burkholderia glumae lipase, suggested that the amino acid substitutions found in the active chimeras were located mostly on the protein model surface [4].

High impact information on PFL_0617

• The neutral lipase from the bacteria Pseudomonas fluorescens, marketed under the trade name LpL-200S, has been crystallized in a form suitable for X-ray diffraction analysis from 35% n-propanol at pH 8 [5].
• We conclude that any lipase causing lipolysis of chylomicrons can stimulate their clearance by the liver, but that lipoprotein lipase has an additional effect on the removal, which is not dependent on its catalytic activity [6].
• Four selected mutants from one round of error-prone PCR mutagenesis, T6, T8, T24, and T35, showed 3.2-, 2.6-, 2.9-, and 3.0-fold increases in the level of secretion of TliA lipase, respectively, but had almost the same level of expression of TliD in the membrane as the strain with the wild-type TliDEF transporter [7].
• When p-nitrophenyl esters and triglyceride substrates of various chain-lengths were examined, the lipase displayed highest activity towards C10 acyl groups [8].
• Addition of EDTA completely abolished lipase activity, indicating that KB-Lip was a Ca2+-dependent lipase [8].

Chemical compound and disease context of PFL_0617

• A genomic DNA library of strain KB700A was introduced into Escherichia coli TG1, and screening on tributyrin-containing agar plates led to the isolation of the lipase gene [8].
• The Legionella lipase activity was found to include free fatty acid release from di- and triacylglycerol substrates, in addition to the previously reported cleavage of monoacylglycerol [9].
• Lipase from Pseudomonas fluorescens (PFL), an enzyme with a great tendency to yield bimolecular aggregates, was immobilized via multipoint covalent attachment on glyoxyl-agarose in the presence of Triton X-100 [10].
• Four commercial preparations: a lipase from Candida cylindracea, an esterase from porcine liver, a lipase from Pseudomonas sp., and a cholesterol esterase from Pseudomonas fluorescens were examined [11].
• Effect of Brij 58 on the hydrolysis of methyl butyrate by lipase from Pseudomonas fluorescens [12].

Biological context of PFL_0617

• With lipase covalently inhibited by the latter inhibitor, lipolysis during perfusions was low or absent [6].
• The dimeric ester of hydroxyhexanoate was the main product of enzymatic hydrolysis of polycaprolactone by P. aeruginosa lipase [13].
• Amino acid sequence analysis of the lipase revealed a potential C-terminal targeting sequence recognized by the ATP-binding cassette (ABC) transporter [14].
• Cloning, expression, and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52 [15].
• The depolymerase is a strongly hydrophobic protein and includes the lipase consensus sequence Gly-X-Ser-X-Gly, which is known for serine hydrolases [16].

Anatomical context of PFL_0617

• In our previous study, the lipase of P. fluorescens SIK W1 was cloned and expressed in Escherichia coli, but it accumulated as inactive inclusion bodies [14].
• The stereoselective acylation of meso polyol 2 by vinyl acetate (solvent and acyl donor) in the presence of porcine pancreas lipase gave the corresponding monoester 5 in good yield (76%) and high enantiomeric purity (ee > 98%) [17].
• The assay was able to detect lipase produced by Ps. fluorescens B52 in SM at 5 degrees C when the cell density exceeded 10(8) colony forming units/ml [18].

Associations of PFL_0617 with chemical compounds

• The lipase-specific consensus sequence G-X1-S-X2-G resided in the amino-terminal part of the protein, and carboxyl-terminal consensus sequences were an L-X-G-G-B-G-B-B-X repeat motif and a so-called aspartate box, respectively, which are both found in proteins secreted by the class I secretion pathway [3].
• When equimolar amounts of trioleoylglycerol and fatty acyl alcohol were incubated with pancreatic lipase, carboxylester lipase, or P. fluorescens lipase, wax esters were synthesized dose-dependently [19].
• Ester synthesis catalyzed by polyethylene glycol-modified lipase in benzene [20].
• In sharp contrast to the hydrolyses of the thiolesters of 2-methyloctanoic acid, two aryl esters of 2-methyloctanoic acid catalyzed by R. miehei lipase hydrolyzed with a bias for the R-configuration [21].
• The modified lipase, in which 55% of the total amino groups in the lipase molecule, was soluble in organic solvents such as benzene, toluene, chloroform and dioxane [20].

Other interactions of PFL_0617

• The lipA gene of Serratia marcescens which encodes an extracellular lipase having no N-terminal signal peptide [22].
• In contrast, the production of another exoenzyme, lipase, is not regulated by the gacA gene [23].
• Alignment of Pseudomonas fluorescens lipase/esterase-coding sequences allowed the design of specific primers for family VI lipases, and the isolation and cloning of the resulting gene estA6 [24].
• Legionella pneumophila genes that encode lipase and phospholipase C activities [9].
• In order to evaluate the pta(phosphotransacetylase) (-) mutant of Escherichia coli as a potential host of foreign lipase expression, the pta(-) mutant HB101 was constructed for the purpose of blocking the acetate synthetic pathway [25].

Analytical, diagnostic and therapeutic context of PFL_0617

• In the absence of any lipase the clearance of chylomicron label from the perfusion medium was slow [6].
• Gene cloning, sequence analysis, purification, and secretion by Escherichia coli of an extracellular lipase from Serratia marcescens [3].
• Localization of the truncated OprF-lipase fusion protein was confirmed by western blot analysis, immunofluorescence microscopy, and whole-cell lipase activity [26].
• The principal lipase-rich fractions from gel filtration represented 6.2% of total lipolytic activity [27].
• Hexane was also a better immobilization medium for A. niger lipase [28].

References