Abstract
Acyl CoA diacylglycerol acyltransferase (DGAT, EC 2.3.120) is recognized as a key player of cellular diacylglycerol metabolism. It catalyzes the terminal, yet the committed step in triacylglycerol synthesis using diacylglycerol and fatty acyl CoA as substrates. The protein sequence of diacylglycerol acyltransferse (DGAT) Type 2B in Moretierella ramanniana var. angulispora (Protein_ID = AAK84180.1) was retrieved from GenBank. However, a structure is not yet available for this sequence. The 3D structure of DGAT Type 2B was modeled using a template structure (PDB ID: 1K30) obtained from Protein databank (PDB) identified by searching with position specific iterative BLAST (PSI-BLAST). The template (PDB ID: 1K30) describes the structure of DGAT from Cucurbita moschata. Modeling was performed using Modeller 9v2 and protein model is hence generated. The DGAT type 2B protein model was subsequently docked with six inhibitors (sphingosine; trifluoroperazine; phosphatidic acid; lysophospatidylserine; KCl; 1, 2-diolein) using AutoDock (a molecular docking program). The binding of inhibitors to the protein model of DGAT type 2B is discussed.
Highlights
The enzyme diacylglycerol acyltransferase (DGAT) [EC 2.3.1.20] catalyses the chain terminating step in triacylglycerol (TG) biosynthesis
We reported the purification of diacylglycerol acyltransferse (DGAT) from the lipid body fraction of the fungus [14]
We describe the binding of the inhibitors with the protein model of DGAT type 2B
Summary
The enzyme diacylglycerol acyltransferase (DGAT) [EC 2.3.1.20] catalyses the chain terminating step in triacylglycerol (TG) biosynthesis. The fungus is known as a potent producer of γ-linolenic acid and essential fatty acids by fermentation [8 -10]. Such oleaginous fungi are expected to exhibit amplified expression of specific mechanisms for TG biosynthesis and TG sequestration in lipid bodies taking advantage of oleaginicity. We reported the purification of DGAT from the lipid body fraction of the fungus [14]. This allowed for further studies on TG biosynthesis. Methodology: DGAT sequence The sequence of the diacylglycerol acyltransferse (DGAT) type 2B from Mortierella ramanniana var. The authors submitted the two protein models for DGAT as follows: (a) DGAT 2B model submitted to Protein Model Database in France during August 2007 (Protein ID: PM 0074978) and (B) DGAT 2A model submitted to Protein Model Database in France during August’ 2007 (Protein ID: PM 0074981)
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call