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Utilization of alcohols by plant and mammalian phospholipase D
Author(s) -
Ella Krishna M.,
Meier Kathryn E.,
Kumar Anil,
Zhang Yanzhi,
Meier G. Patrick
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201761
Subject(s) - phospholipase d , alcohol , chemistry , steric effects , phospholipase a2 , primary alcohol , vascular smooth muscle , primary (astronomy) , enzyme , phospholipase , stereochemistry , butanol , medicinal chemistry , biochemistry , ethanol , smooth muscle , catalysis , biology , physics , astronomy , endocrinology
Abstract The transphosphatidylation reaction is a unique property of phospholipase D (PLD). In this study, the abilities of plant and mammalian PLDs to utilize straight chain and branched alcohols for transphosphatidylation were analyzed and compared. PLD from peanut utilizes C1 to C8 primary alcohols and gives maximal reaction with butanol. In contrast, PLD from A7r5 vascular smooth muscle cells gives maximal reaction with pentanol and does not utilize octanol. Secondary and tertiary alcohols are not substrates for either enzyme. For branched alcohols, activity increases with distance from the alcohol to the branch point. Competition studies indicated that secondary alcohols cannot access the binding pocket. Thus, PLDs have a water/alcohol binding site with defined steric and hydrophobic parameters.