The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase resides at the subunit interface and incorporates catalytically essential acidic residues from separate polypeptides.-Reference-Cited by-同舟云学术

The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase resides at the subunit interface and incorporates catalytically essential acidic residues from separate polypeptides.

Published:1994-01 Issue:2 Volume:269 Page:1217-1221
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Frimpong K.,Rodwell V.W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. The discovery and development of HMG-CoA reductase inhibitors.

2. pH Properties and chemical mechanism of action of 3-hydroxy-3-methylglutaryl coenzyme A reductase

3. Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase.

4. Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.

5. Purification and properties of the catalytic domain of human 3-hydroxy-3-methylglutaryl-CoA reductase expressed in Escherichia coli

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