Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant
Identifieur interne : 000284 ( PascalFrancis/Checkpoint ); précédent : 000283; suivant : 000285Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant
Auteurs : Kenichi Akaji [Japon] ; Hiroyuki Konno [Japon] ; Mari Onozuka [Japon] ; Ayumi Makino [Japon] ; Hiroyuki Saito [Japon] ; Kazuto Nosaka [Japon]Source :
- Bioorganic & medicinal chemistry [ 0968-0896 ] ; 2008.
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Abstract
The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with lle at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a Km of 33.8 μM and kcat of 4753 s-1. Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 106. Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.
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<front><div type="abstract" xml:lang="en">The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with lle at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K<sub>m</sub>
of 33.8 μM and k<sub>cat</sub>
of 4753 s<sup>-1</sup>
. Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10<sup>6</sup>
. Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.</div>
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<fC01 i1="01" l="ENG"><s0>The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with lle at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K<sub>m</sub>
of 33.8 μM and k<sub>cat</sub>
of 4753 s<sup>-1</sup>
. Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10<sup>6</sup>
. Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.</s0>
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<s5>11</s5>
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<s5>12</s5>
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<s5>12</s5>
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<s5>32</s5>
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<s5>32</s5>
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<s4>INC</s4>
<s5>76</s5>
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<s2>FE</s2>
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<s2>FE</s2>
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<fC07 i1="01" i2="X" l="SPA"><s0>Peptidases</s0>
<s2>FE</s2>
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<s2>FE</s2>
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</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fN21><s1>026</s1>
</fN21>
</pA>
</standard>
</inist>
<affiliations><list><country><li>Japon</li>
</country>
</list>
<tree><country name="Japon"><noRegion><name sortKey="Akaji, Kenichi" sort="Akaji, Kenichi" uniqKey="Akaji K" first="Kenichi" last="Akaji">Kenichi Akaji</name>
</noRegion>
<name sortKey="Konno, Hiroyuki" sort="Konno, Hiroyuki" uniqKey="Konno H" first="Hiroyuki" last="Konno">Hiroyuki Konno</name>
<name sortKey="Makino, Ayumi" sort="Makino, Ayumi" uniqKey="Makino A" first="Ayumi" last="Makino">Ayumi Makino</name>
<name sortKey="Nosaka, Kazuto" sort="Nosaka, Kazuto" uniqKey="Nosaka K" first="Kazuto" last="Nosaka">Kazuto Nosaka</name>
<name sortKey="Onozuka, Mari" sort="Onozuka, Mari" uniqKey="Onozuka M" first="Mari" last="Onozuka">Mari Onozuka</name>
<name sortKey="Saito, Hiroyuki" sort="Saito, Hiroyuki" uniqKey="Saito H" first="Hiroyuki" last="Saito">Hiroyuki Saito</name>
</country>
</tree>
</affiliations>
</record>
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