Document Detail


Extracellular lipase from Pseudomonas aeruginosa is an amphiphilic protein.
MedLine Citation:
PMID:  1576157     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) secreted by Pseudomonas aeruginosa PAC1R was purified from cell-free growth medium by preparative isoelectric focusing. After blotting the N-terminal amino acid sequence and the amino acid composition were determined and compared to P. fragi and P. cepacia lipases yielding significant homology between all three species. Additionally, a consensus sequence K-Y-P-i-v-l-V-H-G was identified residing at the N-terminus of Pseudomonas lipases and in the central part of Staphylococcus lipases. Treatment of lipase with the serine-specific inhibitor diethyl p-nitrophenyl phosphate caused a rapid and complete inhibition of enzyme activity indicating the presence of a serine at the catalytic site as expected from lipase consensus sequences. Upon charge-shift electrophoresis the electrophoretic mobility of purified lipase was shifted either anodally or cathodally in the presence of sodium deoxycholate and cetyltrimethylammoniumbromide, respectively. This result demonstrates that extracellular lipase of P. aeruginosa exhibits an amphiphilic character like intrinsic membrane proteins.
Authors:
K E Jaeger; F J Adrian; H E Meyer; R E Hancock; U K Winkler
Related Documents :
2134857 - Isolation and characterization of a proteinaceous inhibitor of microbial proteinases in...
8382297 - Identification of amino acid residues critical for infection with ecotropic murine leuk...
23987337 - Synthesis and properties of fatty acid starch esters.
24491697 - Physicochemical and biochemical properties of honeys from arid regions.
6889107 - Fatty acid synthesis in the arrested rabbit heart during ischemia.
490547 - Structural analogues of l-glutamic acid gamma-(4-hydroxyanilide) and gamma-(3,4-dihydro...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1120     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1992 Apr 
Date Detail:
Created Date:  1992-06-05     Completed Date:  1992-06-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  315-21     Citation Subset:  IM    
Affiliation:
Lehrstuhl für Biologie der Mikroorganismen, Ruhr-Universität, Bochum, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / analysis
Cholic Acids / pharmacology
Detergents / pharmacology
Isoelectric Focusing
Lipase / antagonists & inhibitors,  chemistry*,  isolation & purification
Molecular Sequence Data
Phosphoric Acid Esters / pharmacology
Protein Conformation
Pseudomonas aeruginosa / enzymology*
Sequence Homology, Nucleic Acid
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Cholic Acids; 0/Detergents; 0/Phosphoric Acid Esters; 598-02-7/diethyl phosphate; 75621-03-3/3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate; EC 3.1.1.3/Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The complete amino acid sequence of growth hormone from sturgeon (Acipencer guldenstadti).
Next Document:  Isolation and partial characterization of a high-molecular-weight DNA polymerase from Leishmania mex...