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Article

Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S.

The Journal of biological chemistry - 25 Dec 1991

Ido E, Han H P, Kezdy F J, Tang J

Abstract excerpt

Human immunodeficiency virus type 1 (HIV-1) protease optimally catalyzes in the pH range of 4-6 in contrast to nearly all of the other eukaryotic aspartic proteases, which catalyze best in the pH range of 2-4. A possible structural reason for the higher optimal pH of HIV-1 protease is the absence of a hydrogen bond to the carboxyl group of active-site Asp25, which is nearly universally present in others. To...

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PMID: 1761538

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