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M94A0252.TXT
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1994-10-08
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Document 0252
DOCN M94A0252
TI Analysis of substrate cleavage by recombinant protease of human T cell
leukaemia virus type 1 reveals preferences and specificity of binding.
DT 9412
AU Daenke S; Schramm HJ; Bangham CR; Institute of Molecular Medicine,
Public Health Laboratory, John; Radcliffe Hospital, Headington, Oxford,
U.K.
SO J Gen Virol. 1994 Sep;75 ( Pt 9):2233-9. Unique Identifier : AIDSLINE
MED/94358721
AB Human T cell leukaemia virus type 1 (HTLV-1) protease (PR14) was
expressed in bacteria and purified by gel filtration. A continuous
spectrophotometric assay was used to measure the kinetic parameters of
substrate hydrolysis by PR14. Several peptide substrates containing
HTLV-1 sequences known to be cleaved by PR14 were used. Cleavage
analysis showed that the affinity with which PR14 binds these substrates
is higher than that previously reported for HTLV-1 Gag peptides. Also,
the affinities of peptides containing the sites involved in autocleavage
of protease from its precursor are higher than for the peptides
containing sites required for structural protein maturation. This
suggests that the autocatalysis of protease from its own precursor has
priority over other cleavage reactions and supports similar observations
of an ordered hierarchy of processing events by retroviral proteases. As
the N- and C-terminal regions of retroviral aspartic proteases are known
to contribute to stability of the dimer by forming antiparallel
beta-strands, short peptides corresponding to these terminal sequences
of HTLV-1 protease were tested for their ability to inhibit cleavage of
substrates by PR14. Inhibition was seen with a C-terminal peptide
corresponding exactly to the C-terminal 11 amino acids of the processed
PR14, whereas a peptide containing a sequence situated further from the
C terminus was less effective. An inhibitor of the protease of human
immunodeficiency virus type 1, Ro 31-8959, was found to be a poor
inhibitor of PR14.
DE Amino Acid Sequence Aspartic Proteinases/*METABOLISM Binding Sites
Cloning, Molecular Comparative Study Escherichia coli
HIV-1/*ENZYMOLOGY HTLV-I/*ENZYMOLOGY Kinetics Molecular Sequence Data
Molecular Weight Peptide Peptidohydrolases/CHEMISTRY/ISOLATION &
PURIF/*METABOLISM Protease Inhibitors/PHARMACOLOGY Recombinant
Proteins/CHEMISTRY/ISOLATION & PURIF/METABOLISM Substrate Specificity
Support, Non-U.S. Gov't JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).