Journal article
Utilization of alcohols by plant and mammalian phospholipase D
IUBMB life, Vol.41(4), pp.715-724
04/1997
Handle:
https://hdl.handle.net/2376/108044
PMID: 9111933
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.
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Details
- Title
- Utilization of alcohols by plant and mammalian phospholipase D
- Creators
- Krishna M EllaKathryn E MeierAnil KumarYanzhi ZhangG. Patrick Meier
- Publication Details
- IUBMB life, Vol.41(4), pp.715-724
- Academic Unit
- Pharmaceutical Sciences, Department of
- Publisher
- Informa Healthcare; UK
- Number of pages
- 10
- Identifiers
- 99900547288501842
- Language
- English
- Resource Type
- Journal article