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

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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...

Topics

Alanine
Amino Acid Sequence
Base Sequence
Binding Sites
Catalysis
DNA, Viral
Electrophoresis, Polyacrylamide Gel
Genes, Synthetic
Genetic Vectors
HIV Protease
Hydrogen
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutation
Polymerase Chain Reaction
Serine

Source

Open in PubMed

Identifiers

PMID: 1761538

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1761538-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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