Document 0120
 DOCN  M95A0120
 TI    Cloning, bacterial expression, and characterization of the Mason-Pfizer
       monkey virus proteinase.
 DT    9510
 AU    Hruskova-Heidingsfeldova O; Andreansky M; Fabry M; Blaha I; Strop P;
       Hunter E; Institute of Organic Chemistry and Biochemistry, Czech Academy
       of; Sciences, Prague.
 SO    J Biol Chem. 1995 Jun 23;270(25):15053-8. Unique Identifier : AIDSLINE
       MED/95318063
 AB    We have cloned and expressed the 3' region of the Mason-Pfizer monkey
       virus pro gene in Escherichia coli. The recombinant 26-kDa precursor
       undergoes rapid self-processing both in E. coli and in vitro at the NH2
       terminus, yielding a proteolytically active 17-kDa protein, p17. This
       initial cleavage is followed in vitro by a much slower self-processing
       that leads to emergence of proteolytically active p12 and a
       COOH-terminal cleavage product p5. We have found the NH2-terminal
       processing site of both the p17 and p12 to be identical and similar to
       the amino terminus of the mouse mammary tumor virus proteinase. We have
       also identified the COOH-terminal processing site of the p12 form. Using
       purified recombinant proteins and synthetic oligopeptide substrates
       based on naturally occurring retroviral processing sites, we have
       determined the enzymatic activity and specificity of the Mason-Pfizer
       monkey virus proteinase to be more closely related to that of
       myeloblastosis-associated virus proteinase rather than that of the Human
       immunodeficiency virus type 1 proteinase. Inhibition studies using
       peptide inhibitors support these results.
 DE    Amino Acid Sequence  Chromatography, Gel  Cloning, Molecular
       Comparative Study  Enzyme Precursors/METABOLISM  Escherichia coli/DRUG
       EFFECTS/METABOLISM  Gene Expression  Genes, Viral  HIV
       Protease/METABOLISM  HIV Protease Inhibitors/*PHARMACOLOGY  Isopropyl
       Thiogalactoside/PHARMACOLOGY  Mason-Pfizer Monkey
       Virus/*ENZYMOLOGY/GENETICS/ISOLATION & PURIF  Molecular Sequence Data
       Molecular Weight  Peptide Peptidohydrolases/BIOSYNTHESIS/*METABOLISM
       Protease Inhibitors/PHARMACOLOGY  Protein Processing, Post-Translational
       Recombinant Proteins/BIOSYNTHESIS/ISOLATION & PURIF/METABOLISM
       Restriction Mapping  Support, Non-U.S. Gov't  Support, U.S. Gov't,
       P.H.S.  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).