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IJBT Vol.11 [2012] >
IJBT Vol.11(1) [January 2012] >
| Title: | Molecular cloning and structural characterization of HMG-CoA reductase gene from Catharanthus roseus (L.) G. Donn. cv. Albus |
| Authors: | Abdin, M Z
Kiran, U
Aquil, S |
| Keywords: | Catharanthus roseus
HMG-CoA Reductase
Isoprenoid Biosynthesis
Mevalonate Pathway
PS2 Server
Secondary Plant Metabolites |
| Issue Date: | Jan-2012 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | The
3-hydroxy-3-methyl glutaryl-CoA reductase (HMGR) catalyzes the conversion of
HMG-CoA to mevalonate, the first committed step in isoprenoid biosynthesis
pathway in plants. HMG-CoA reductase gene was amplified from the Catharanthus roseus (L.) G. Donn. cv.
Albus by polymerase chain reaction (PCR) with primers designed using published
sequence of HMG-CoA reductase c-DNA of C. roseus cv. Little Delicata (Acc. No. M96068). PS2 SERVER was used to generate three dimensional (3-D) structure of the
enzyme using human HMG-CoA reductase as template. The
structure was evaluated at various web interfaced
servers, i.e., PROCHEK, Profunc and PDBsum, for checking the stereo interfaced
quality of the structure in terms of bonds, bond angles, dihedral angles,
structural as well as functional domains. The generated model was visualized
using the Rasmol. The results of these studies revealed that HMG-CoA reductase
gene from cv. Albus had 99% sequence
homology with hmgr cDNA of cv. Little Delicata. The amino acid sequence of the HMGR protein of cv.
Albus was found closely
related to the members of the family Solanaceae and distantly related to the members
of the families Euphorbiaceae and Brassicaceae. The enzyme has N-terminal
transmembrane domain and a C-terminal catalytic domain with active sites that
can bind to HMG-CoA and NADPH2. The fold of the substrate domain is
unique and resembles the prism with 28-residue helix forming the central core.
The homology model of enzyme generated in the present study, hence, could be
used in determining the mechanistic function of this important class of
proteins. |
| Page(s): | 16-22 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0967 (Online); 0972-5849 (Print) |
| Source: | IJBT Vol.11(1) [January 2012]
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