Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase (PDAT) devoid of its membrane anchor region is a soluble and active enzyme retaining its substrate specificities

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1771, Issue 12, 2007, Pages 1457-1463

  Ghosal, Alokesh ^a   Banas, Antoni ^b   Ståhl, Ulf ^b   Dahlqvist, Anders ^a   Lindqvist, Ylva ^c   Stymne, Sten ^b  

^a Scandinavian Biotechnology Research (ScanBiRes) AB   (Sweden)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Deletion; Membrane spanning; PDAT; Phospolipid:diacylglycerol acyltransferase; Transacylation; Yeast

Indexed keywords

ALCOHOL OXIDASE; DIACYLGLYCEROL; DIACYLGLYCEROL ACYLTRANSFERASE; ENZYME; LIPID; MATING HORMONE ALPHA FACTOR; MEMBRANE ENZYME; METHANOL; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID;

ACYLATION; ARTICLE; CULTURE MEDIUM; DEGLYCOSYLATION; ENZYME SPECIFICITY; GLYCOSYLATION; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SECRETION; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

ACYLTRANSFERASES; ANIMALS; GLYCOSYLATION; LIPID METABOLISM; LIPIDS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY;

PICHIA PASTORIS; SACCHAROMYCES CEREVISIAE;

EID: 38349033129     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2007.10.007     Document Type: Article

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