Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease

Jeong Kyu Bang; Kenta Teruya; Saburo Aimoto; Hiroyuki Konno; Kazuto Nosaka; Tadashi Tatsumi; Kenichi Akaji

doi:10.1007/s10989-006-9062-z

Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease

Jeong Kyu Bang, Kenta Teruya, Saburo Aimoto, Hiroyuki Konno, Kazuto Nosaka, Tadashi Tatsumi, Kenichi Akaji

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

Substrate specificities for recognition at the PR/p3 site of HTLV-1 protease were clarified using small libraries of substrate peptides. Specificities at P₁ and P₁′ positions were examined by parallel synthesis/digestion of synthetic peptides covering the PR/p3 site (KGPPVILPIQA). Specificities at P₂ to P₄ positions were examined by split and mix syntheses of olefin-peptide libraries containing the substrate sequence (PPVILPIQ). The solid-phase Horner-Emmons reaction was successfully applied to syntheses of multi-component substrates for library preparation. From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HTLV-1 PR), it was found for the first time that the preference for Pro at the P₁′ position and for Ile at the P₂ position is unique for this enzyme.

Original language	English
Pages (from-to)	173-179
Number of pages	7
Journal	International Journal of Peptide Research and Therapeutics
Volume	13
Issue number	1-2
DOIs	https://doi.org/10.1007/s10989-006-9062-z
Publication status	Published - 2007 Jun
Externally published	Yes

Keywords

HTLV-1
Horner-Emmons reaction
Solid-phase synthesis
Substrate specificity

ASJC Scopus subject areas

Analytical Chemistry
Bioengineering
Biochemistry
Molecular Medicine
Drug Discovery

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title = "Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease",

abstract = "Substrate specificities for recognition at the PR/p3 site of HTLV-1 protease were clarified using small libraries of substrate peptides. Specificities at P1 and P1′ positions were examined by parallel synthesis/digestion of synthetic peptides covering the PR/p3 site (KGPPVILPIQA). Specificities at P2 to P4 positions were examined by split and mix syntheses of olefin-peptide libraries containing the substrate sequence (PPVILPIQ). The solid-phase Horner-Emmons reaction was successfully applied to syntheses of multi-component substrates for library preparation. From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HTLV-1 PR), it was found for the first time that the preference for Pro at the P1′ position and for Ile at the P2 position is unique for this enzyme.",

keywords = "HTLV-1, Horner-Emmons reaction, Solid-phase synthesis, Substrate specificity",

author = "Bang, {Jeong Kyu} and Kenta Teruya and Saburo Aimoto and Hiroyuki Konno and Kazuto Nosaka and Tadashi Tatsumi and Kenichi Akaji",

year = "2007",

month = jun,

doi = "10.1007/s10989-006-9062-z",

language = "English",

volume = "13",

pages = "173--179",

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T1 - Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease

AU - Bang, Jeong Kyu

AU - Teruya, Kenta

AU - Aimoto, Saburo

AU - Konno, Hiroyuki

AU - Nosaka, Kazuto

AU - Tatsumi, Tadashi

AU - Akaji, Kenichi

PY - 2007/6

Y1 - 2007/6

N2 - Substrate specificities for recognition at the PR/p3 site of HTLV-1 protease were clarified using small libraries of substrate peptides. Specificities at P1 and P1′ positions were examined by parallel synthesis/digestion of synthetic peptides covering the PR/p3 site (KGPPVILPIQA). Specificities at P2 to P4 positions were examined by split and mix syntheses of olefin-peptide libraries containing the substrate sequence (PPVILPIQ). The solid-phase Horner-Emmons reaction was successfully applied to syntheses of multi-component substrates for library preparation. From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HTLV-1 PR), it was found for the first time that the preference for Pro at the P1′ position and for Ile at the P2 position is unique for this enzyme.

AB - Substrate specificities for recognition at the PR/p3 site of HTLV-1 protease were clarified using small libraries of substrate peptides. Specificities at P1 and P1′ positions were examined by parallel synthesis/digestion of synthetic peptides covering the PR/p3 site (KGPPVILPIQA). Specificities at P2 to P4 positions were examined by split and mix syntheses of olefin-peptide libraries containing the substrate sequence (PPVILPIQ). The solid-phase Horner-Emmons reaction was successfully applied to syntheses of multi-component substrates for library preparation. From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HTLV-1 PR), it was found for the first time that the preference for Pro at the P1′ position and for Ile at the P2 position is unique for this enzyme.

KW - HTLV-1

KW - Horner-Emmons reaction

KW - Solid-phase synthesis

KW - Substrate specificity

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JO - Letters in Peptide Science

JF - Letters in Peptide Science

SN - 1573-3149

IS - 1-2

ER -

Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease

Abstract

Keywords

ASJC Scopus subject areas

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