Characterization of acyl-coenzyme A: diacylglycerol acyltransferase (DGAT) enzyme of human small intestine
J. physiol. biochem
; 67(2): 259-264, jun. 2011. ilus
Article
in English
| IBECS
| ID: ibc-122626
Responsible library:
ES1.1
Localization: BNCS
RESUMEN
No disponible
ABSTRACT
Acyl-coenzyme Adiacylglycerol acyltransferase (DGAT) enzyme plays a significant role in dietary triacylglycerol (TAG) absorption in the small intestine. However, the characteristics of human intestinal DGAT enzyme have not been examined in detail. The aim of our study was to characterize the human intestinal DGAT enzyme by examining acyl-CoA specificity, temperature dependency, and selectivity for 1,2-diacylglycerol (DAG) or 1,3-DAG. We detected DGAT activity of human intestinal microsome and found that the acyl-CoA specificity and temperature dependency of intestinal DGAT coincided with those of recombinant human DGAT1. To elucidate the selectivity of human intestinal DGAT to 1,2-DAG or 1,3-DAG, we conducted acyl-coenzyme Amonoacylglycerol acyltransferase assays using 1- or 2-monoacylglycerol (MAG) as substrates. When 2-MAG was used as acyl acceptor, both 1,2-DAG and TAG were generated; however, when 1-MAG was used, 1,3-DAG was predominantly observed and little TAG was detected. These findings suggest that human small intestinal DGAT, which is mainly encoded by DGAT1, utilizes 1,2-DAG as the substrate to form TAG. This study will contribute to understand the lipid absorption profile in the small intestine (AU)
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Collection:
National databases
/
Spain
Database:
IBECS
Main subject:
Acyl Coenzyme A
/
Diacylglycerol O-Acyltransferase
/
Intestine, Small
Limits:
Humans
Language:
English
Journal:
J. physiol. biochem
Year:
2011
Document type:
Article
Institution/Affiliation country:
Dainippon-Sumitomo Pharma Co/Japan
/
Osaka City University/Japan