NDLI: Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.

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Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Louis, J. M. Parris, K. D. Jerina, D. M. Kimmel, A. R. Nashed, N. T.
Description	Author Affiliation: Louis JM ( Laboratory of Cellular and Developmental Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.);
Abstract	Upon renaturation, the polyprotein MBP-delta TF-Protease-delta Pol, consisting of HIV-1 protease and short native sequences from the trans-frame protein (delta TF) and the polymerase (delta Pol) fused to the maltose-binding protein (MBP) of Escherichia coli, undergoes autoprocessing to produce the mature protease in two steps. The initial step corresponds to cleavage of the N-terminal sequence to release the protein intermediate Protease-delta Pol, which has enzymatic activity comparable to that of the mature enzyme. Subsequently, the mature enzyme is formed by a slower cleavage at the C terminus. The rate of increase in enzymatic activity is identical to that of the appearance of MBP-delta TF and the disappearance of the MBP-delta TF-Protease-delta Pol. Initial rates are linearly dependent on the protein concentration, indicating that the N-terminal cleavage is first-order in protein concentration. The reaction is competitively inhibited by pepstatin A and has a pH rate profile similar to that of the mature enzyme. These results and molecular modeling studies are discussed in terms of a mechanism in which a dimeric full-length fusion protein must form prior to rate-limiting intramolecular cleavage of the N-terminal sequence that leads to an increase in enzymatic activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	ATP-Binding Cassette Transporters Escherichia Coli Proteins Fusion Proteins, Gag-pol Metabolism HIV Protease Biosynthesis HIV-1 Enzymology Monosaccharide Transport Proteins Amino Acid Sequence Carrier Proteins Escherichia Coli Chemistry Hydrogen-Ion Concentration Kinetics Maltose-Binding Proteins Models, Molecular Molecular Sequence Data Oligopeptides Pepstatins Pharmacology Protein Folding Protein Structure, Secondary Substrate Specificity Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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