Document Detail

Purification and characterization of phospholipase B from Candida utilis.
MedLine Citation:
PMID:  16495653     Owner:  NLM     Status:  MEDLINE    
Phospholipase B (PLB) from the asporogenous yeast Candida utilis was purified to homogeneity from a culture broth. The apparent molecular mass was 90-110 kDa by SDS-PAGE. The enzyme had two pH optima, one acidic (pH 3.0) and the other alkaline (pH 7.5). At acidic pH the enzyme hydrolyzed all phospholipids tested without metal ions. On the other hand, the PLB showed substrate specificity and required metal ions for alkaline activity. The cDNA sequence of the PLB was analyzed by a combination of several PCR procedures. The PLB encoded a protein consisting of 643 amino acids. The amino acid sequence contained a lipase consensus sequence (GxSxG) and catalytic arginine and aspartic acid motifs which were identified as the catalytic triad in the PLB from Kluyveromyces lactis, suggesting that the catalytic mechanism of the PLB is similar to that of cytosolic phospholipase A(2) (cPLA(2)), found in mammalian tissues.
Shuji Fujino; Daigo Akiyama; Satoko Akaboshi; Tomonari Fujita; Yasuo Watanabe; Youichi Tamai
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  70     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-02-23     Completed Date:  2006-07-20     Revised Date:  2009-11-03    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  377-86     Citation Subset:  IM    
Laboratory of Food Biochemistry, Department of Bioresources, Faculty of Agriculture, Ehime University, Japan.
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MeSH Terms
Acyltransferases / metabolism
Amino Acid Sequence
Candida / enzymology*,  genetics
Cations / chemistry
Conserved Sequence
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Lysophospholipase / chemistry,  genetics,  isolation & purification*,  metabolism*
Metals / chemistry,  pharmacology
Molecular Sequence Data
Molecular Weight
Sequence Alignment
Substrate Specificity
Reg. No./Substance:
0/Cations; 0/Metals; EC 2.3.-/Acyltransferases; EC

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

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