当前位置： SCI文献检索 > APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY期刊下所有文献 > Recombinant 3-Hydroxy 3-Methyl Glutaryl-CoA Reductase from Candida glabrata (Rec-CgHMGR) Obtained by Heterologous Expression, as a Novel Therapeutic Target Model for Testing Synthetic Drugs.

Recombinant 3-Hydroxy 3-Methyl Glutaryl-CoA Reductase from Candida glabrata (Rec-CgHMGR) Obtained by Heterologous Expression, as a Novel Therapeutic Target Model for Testing Synthetic Drugs.

Abstract：

:The enzyme 3-hydroxy-3-methyl-glutaryl CoA reductase (HMGR) is a glycoprotein of the endoplasmic reticulum that participates in the mevalonate pathway, the precursor of cholesterol in human and ergosterol in fungi. This enzyme has three domains: transmembrane, binding, and soluble. In this study, we expressed and purified the soluble fraction of the HMGR enzyme from Candida glabrata (CgHMGR) in an Escherichia coli heterologous system and used it as a model for studying its inhibitory activity. The soluble fraction of CgHMGR was fused to the maltose binding protein (MBP), purified, and characterized. Optimal pH was 8.0, and its optimal temperature activity was 37 °C. The k m and V max for the HMG-CoA were 6.5 μM and 2.26 × 10-3 μM min-1, respectively. Recombinant CgHMGR was inhibited by simvastatin presenting an IC50 at 14.5 μM. In conclusion, our findings suggest that the recombinant HMGR version from C. glabrata may be used as a study model system for HMGR inhibitors such as statins and newly synthesized inhibitor compounds that might be used in the treatment of hypercholesterolemia or mycosis.

journal_name

Appl Biochem Biotechnol

journal_title

Applied biochemistry and biotechnology

authors

Andrade-Pavón D,Cuevas-Hernández RI,Trujillo-Ferrara JG,Hernández-Rodríguez C,Ibarra JA,Villa-Tanaca L

doi

10.1007/s12010-017-2412-9

subject

Has Abstract

pub_date

2017-08-01 00:00:00

pages

1478-1490

issue

4

eissn

0273-2289

issn

1559-0291

pii

10.1007/s12010-017-2412-9

journal_volume

182

pub_type

杂志文章

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