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(Ala-Arg-Leu-Gln-NH)2-rhodamine
rhodamine 110 + (Ala-Arg-Leu-Gln-NH)-rhodamine
-
-
-
-
?
(CAL fluor red 610)-TSAVLQSGFRK(BHQ1) + H2O
(CAL fluor red 610)-TSAVLQ + SGFRK(BHQ1)
-
-
-
-
?
2-aminobenzoyl-SVTLQSG-Tyr(NO2)Arg + H2O
?
-
-
-
-
?
2-aminobenzoyl-TSAVLQSGFRK-2,4-dinitrophenyl amide + H2O
2-aminobenzoyl-TSAVLQ + SGFRK-2,4-dinitrophenyl amide
-
-
-
-
?
AAVLQSGF-NH2 + H2O
AAVLQ + SGF-NH2
-
-
-
-
?
Abz-LQSGFRK(Dnp)NH2 + H2O
Abz-LQ + SGFRK(Dnp)NH2
-
-
-
-
?
Abz-LYQPPQTSITSAVLQSGFRK(Dnp)NH2 + H2O
Abz-LYQPPQTSITSAVLQ + SGFRK(Dnp)NH2
-
-
-
-
?
Abz-QTSITSAVLQSGFRK(Dnp)NH2 + H2O
Abz-QTSITSAVLQ + SGFRK(Dnp)NH2
-
-
-
-
?
Abz-SAVLQSGFRK(Dnp)NH2 + H2O
Abz-SAVLQ + SGFRK(Dnp)NH2
-
-
-
-
?
Abz-SAVLQSGFRKMAFPSGK(Dnp)NH2 + H2O
Abz-SAVLQ + SGFRKMAFPSGK(Dnp)NH2
-
-
-
-
?
Abz-SAVLQSGFRKMAK(Dnp)NH2 + H2O
Abz-SAVLQ + SGFRKMAK(Dnp)NH2
-
-
-
-
?
Abz-SAVLQSGK(Dnp)NH2 + H2O
Abz-SAVLQ + SGK(Dnp)NH2
-
-
-
-
?
Abz-SGADVLYQPPQTSITSAVLQSGFRK(Dnp)NH2 + H2O
Abz-SGADVLYQPPQTSITSAVLQ + SGFRK(Dnp)NH2
-
-
-
-
?
Abz-VLQSGFRK(Dnp)NH2 + H2O
Abz-VLQ + SGFRK(Dnp)NH2
-
-
-
-
?
acetyl-TSAVLH-7-amido-4-carbamoyl-coumarin + H2O
acetyl-TSAVLH + 7-amino-4-carbamoyl-coumarin
-
SARS-CoV 3Clpro prefers Gln over His in P1 position. Unlike SARS-CoV 3Clpro, His is strongly preferred in the P1 position by 3C-like proteases from infectious bronchitis virus murine hepatitis virus
-
-
?
acetyl-TSTKLQ-7-amido-4-carbamoyl-coumarin + H2O
acetyl-TSTKLQ + 7-amino-4-carbamoyl-coumarin
-
optimized fluorogenic peptide substrate. The enzyme exhibits a strong preference for P1 Gln containing substrates and P2 Leu containing substrates
-
-
?
ATVRLQAGNAT + H2O
ATVRLQ + AGNAT
-
-
-
-
?
AVLQS-NH2 + H2O
AVLQ + L-serinamide
-
-
-
-
?
AVLQSE-NH2 + H2O
AVLQ + Ser-Glu-NH2
-
-
-
-
?
AVLQSGF-NH2 + H2O
AVLQ + SGF-NH2
-
-
-
-
?
coronavirus polyprotein + H2O
?
cyan fluorescent protein-TSAVLQSGFRKM-yellow fluorescent protein + H2O
cyan fluorescent protein-TSAVLQ + SGFRKM-yellow fluorescent protein
-
-
-
-
?
Dabcyl-KNSTLQSGLRKE-EDANS + H2O
Dabcyl-KNSTLQ + SGLRKE-EDANS
-
-
-
-
?
dabcyl-KTSAVLQSGFRKME-EDANS + H2O
?
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
Dabcyl-KTSAVLQSGFRKME-EDANS-amide + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS-amide
-
-
-
?
Dabcyl-KTSAVLQSGFRKMQ-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKMQ-EDANS
-
-
-
-
?
DABCYL-Lys-Asn-Ser-Thr-Leu-Gln-Ser-Gly-Leu-Arg-Lys-Glu-EDANS + H2O
DABCYL-Lys-Asn-Ser-Thr-Leu-Gln + Ser-Gly-Leu-Arg-Lys-Glu-EDANS
-
-
-
-
?
DABCYL-Lys-Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-Met-Glu-EDANS + H2O
DABCYL-Lys-Thr-Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys-Met-Glu-EDANS
-
-
-
-
?
DABCYL-TSAVLQSGFRKME-EDANS + H2O
DABCYL-TSAVLQ + SGFRKME-EDANS
EDANS-VNSTLQSGLRK-(Dabcyl)-M + H2O
EDANS-VNSTLQ + SGLRK-(Dabcyl)-M
-
-
-
-
?
FAVLQSGF + H2O
FAVLQ + SGF
-
-
-
-
?
FVRLQSGF + H2O
FVRLQ + SGF
-
-
-
-
?
FVVLQSGF + H2O
FVVLQ + SGF
-
-
-
-
?
FYPKLQASQAW + H2O
FYPKLQ + ASQAW
-
-
-
-
?
GPFVDRQTAQAAGTDT-NH2 + H2O
?
-
1% of the activity with TSAVLQSGFRK-NH2
-
-
?
H-Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-NH2 + H2O
?
-
-
-
?
H-Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-NH2 + H2O
H-Thr-Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys-NH2
KVATVQSKMSD + H2O
KVATVQ + SKMSD
KVATVQSKMSD-NH2
?
-
undecapeptide containing the non-canonical P3/P4 cleavage site of 3CL protease, 6% of the activity with TSAVLQSGFRK-NH2
-
-
?
L-Thr-L-Ser-L-Ala-L-Val-L-Leu-L-Gln-4-nitroanilide + H2O
L-Thr-L-Ser-L-Ala-L-Val-L-Leu-L-Gln + 4-nitroaniline
-
-
-
-
?
LAVLQSGF-NH2 + H2O
LAVLQ + SGF-NH2
-
-
-
-
?
LQSG-NH2 + H2O
Leu-Gln + Ser-Gly-NH2
-
-
-
-
?
MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2 + H2O
?
FRET peptide substrate
-
-
?
MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2 + H2O
MCA-AVLQ + SGFR-Lys(Dnp)-Lys-NH2
-
-
-
?
MCAAVLQSGFR-Lys(Dnp)-Lys-NH2 + H2O
MCAAVLQ + Ser-Gly-Phe-Arg-Lys(Dnp)-Lys-NH2
-
-
-
-
?
N-methylanthranilyl-TSAVLQSGFRK(2,4-dinitrophenyl) + H2O
?
-
-
-
?
NRATLQAIASE + H2O
NRATLQ + AIASE
NVATLQAENVT + H2O
NVATLQ + AENVT
o-aminobenzoyl-TSAVLQSGFRK-2,4-dinitrophenyl amide + H2O
o-aminobenzoyl-TSAVLQSGFRK + 2,4-dinitroaniline
-
-
-
-
?
o-aminobenzoyl-TSAVLQSGFRY(3-NO2)G + H2O
o-aminobenzoyl-TSAVLQ + SGFRY(3-NO2)G
-
-
-
-
?
PATVLQAVGAC + H2O
PATVLQ + AVGAC
-
-
-
-
?
PHTVLQAVGAC + H2O
PHTVLQ + AVGAC
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-
-
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?
pp1a + H2O
?
cleavage of a viron polyprotein
-
-
?
pp1ab + H2O
?
cleavage of a viron polyprotein
-
-
?
REPLMQSADAS + H2O
REPLMQ + SADAS
SAALQSGF-NH2 + H2O
SAALQ + SGF-NH2
-
-
-
-
?
SAKLQSGF-NH2 + H2O
SAKLQ + SGF-NH2
-
-
-
-
?
SALLQSGF-NH2 + H2O
SALLQ + SGF-NH2
-
-
-
-
?
SARS-CoV Trx/GST-tagged C145A 3CLpro mutant + 2 H2O
Trx-10aa + C145A 3CLpro mutant + 10aa-GST
SARS-CoV-2 Trx/GST-tagged C145A 3CLpro mutant + 2 H2O
Trx-10aa + C145A 3CLpro mutant + 10aa-GST
SATLQSGF-NH2 + H2O
SATLQ + SGF-NH2
-
-
-
-
?
SAVAQSGF-NH2 + H2O
SAVAQ + SGF-NH2
-
-
-
-
?
SAVFQSGF-NH2 + H2O
SAVMQ + SGF-NH2
-
-
-
-
?
SAVIQSGF-NH2 + H2O
SAVIQ + SGF-NH2
-
-
-
-
?
SAVKLQNNELS + H2O
SAVKLQ + NNELS
SAVLESGF-NH2 + H2O
SAVLE + SGF-NH2
-
-
-
-
?
SAVLKSGF-NH2 + H2O
SAVLK + SGF-NH2
-
-
-
-
?
SAVLNSGF-NH2 + H2O
SAVLN + SGF-NH
-
-
-
-
?
SAVLQAGF-NH2 + H2O
SAVLQ + AGF-NH2
-
-
-
-
?
SAVLQEGFRK + H2O
SAVLQ + EGFRK
-
the cleavage rate of the mutant enzyme T25G is remarkably higher compared to the wild type enzyme
-
-
?
SAVLQFGFRK + H2O
SAVLQ + FGFRK
-
the cleavage rate of the mutant enzyme T25G is remarkably higher compared to the wild type enzyme
-
-
?
SAVLQGGF-NH2 + H2O
SAVLQ + GGF-NH2
-
-
-
-
?
SAVLQGGFRK + H2O
SAVLQ + GGFRK
-
the cleavage rate of the mutant enzyme T25G is similar to the wild type enzyme
-
-
?
SAVLQHGFRK + H2O
SAVLQ + HGFRK
-
low activity
-
-
?
SAVLQKGFRK + H2O
SAVLQ + KGFRK
-
low activity
-
-
?
SAVLQLGF-NH2 + H2O
SAVLQ + LGF-NH2
-
-
-
-
?
SAVLQLGFRK + H2O
SAVLQ + LGFRK
-
the cleavage rate of the mutant enzyme T25G is remarkably higher compared to the wild type enzyme
-
-
?
SAVLQMGFRK + H2O
SAVLQ + MGFRK
-
the cleavage rate of the mutant enzyme T25G is remarkably higher compared to the wild type enzyme
-
-
?
SAVLQSGF-NH2 + H2O
SAVLQ + SGF-NH2
-
-
-
-
?
SAVLQSGFRK + H2O
SAVLQ + SGFRK
SAVLQWGFRK + H2O
SAVLQ + WGFRK
-
low activity
-
-
?
SAVMQSGF-NH2 + H2O
SAVMQ + SGF-NH2
-
-
-
-
?
SAVRQSGF-NH2 + H2O
SAVRQ + SGF-NH2
-
-
-
-
?
SAVVQSGF-NH2 + H2O
SAVVQ + SGF-NH2
-
-
-
-
?
Ser-Ala-Val-Leu-Gln-Leu-Gly-Phe-Arg-Lys + H2O
Ser-Ala-Val-Leu-Gln + Leu-Gly-Phe-Arg-Lys
-
substrate for T25G mutant protein
-
-
?
Ser-Ala-Val-Leu-Gln-Met-Gly-Phe-Arg-Lys + H2O
Ser-Ala-Val-Leu-Gln + Met-Gly-Phe-Arg-Lys
-
-
-
-
?
Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys + H2O
Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys
-
-
-
-
?
SGVTFQGKFKK + H2O
SGVTFQ + GKFKK
SITSAVLQ-p-nitroanilide + H2O
?
-
-
-
-
?
SITSAVLQ-p-nitrophenyl ester + H2O
?
-
-
-
-
?
SITSAVLQSGFRKMA + H2O
?
-
-
-
-
?
SLVLQSGF-NH2 + H2O
SLVLQ + SGF-NH2
-
-
-
-
?
STVLQSGF-NH2 + H2O
STVLQ + SGF-NH2
-
-
-
-
?
SVVLQSGF-NH2 + H2O
SVVLQ + SGF-NH2
-
-
-
-
?
SWTSAVAQSGFRKWA + H2O
SWTSAVAQ + SGFRKWA
less than 10% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVCQSGFRKWA + H2O
SWTSAVCQ + SGFRKWA
less than 1% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVFQSGFRKWA + H2O
SWTSAVFQ + SGFRKWA
about 70% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVHQSGFRKWA + H2O
SWTSAVHQ + SGFRKWA
less than 5% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVIQSGFRKWA + H2O
SWTSAVIQ + SGFRKWA
about 45% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVLQSGFRKWA + H2O
?
-
-
-
-
?
SWTSAVLQSGFRKWA + H2O
SWTSAVLQ + SGFRKWA
100% activity
-
-
?
SWTSAVMQSGFRKWA + H2O
SWTSAVMQ + SGFRKWA
about 58% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVNQSGFRKWA + H2O
SWTSAVNQ + SGFRKWA
less than 1% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVPQSGFRKWA + H2O
SWTSAVPQ + SGFRKWA
about 10% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVQQSGFRKWA + H2O
SWTSAVQQ + SGFRKWA
less than 5% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVSQSGFRKWA + H2O
SWTSAVSQ + SGFRKWA
less than 1% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVTQSGFRKWA + H2O
SWTSAVTQ + SGFRKWA
less than 5% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVVQSGFRKWA + H2O
SWTSAVVQ + SGFRKWA
about 55% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVWQSGFRKWA + H2O
SWTSAVWQ + SGFRKWA
less than 5% activity compared to SWTSAVLQSGFRKWA
-
-
?
SWTSAVYQSGFRKWA + H2O
SWTSAVYQ + SGFRKWA
less than 5% activity compared to SWTSAVLQSGFRKWA
-
-
?
TAVLQSGF + H2O
TAVLQ + SGF
-
lowest activity
-
-
?
TAVLQSGF-NH2 + H2O
TAVLQ + SGF-NH2
-
-
-
-
?
TFTRLQSLENV + H2O
TFTRLQ + SLENV
-
-
-
-
?
Thr-Ser-Ala-Val-Leu-Gln-4-nitroanilide + H2O
Thr-Ser-Ala-Val-Leu-Gln + 4-nitroaniline
-
-
-
-
?
Thr-Ser-Ala-Val-Leu-Gln-p-nitroanilide + H2O
Thr-Ser-Ala-Val-Leu-Gln + p-nitroaniline
-
-
-
-
?
Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys + H2O
Thr-Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys
-
-
-
?
Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-NH2 + H2O
Thr-Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys-NH2
-
-
-
-
?
TSAVLQ-4-nitroanilide + H2O
TSAVLQ + 4-nitroaniline
-
-
-
?
TSAVLQSGFRK-NH2 + H2O
TSAVLQ + SGFRK-NH2
TVILQAGF + H2O
TVILQ + Ala-Gly-Phe
-
-
-
-
?
TVKLQAGF + H2O
TVKLQ + Ala-Gly-Phe
-
-
-
-
?
TVKLQAGF-NH2 + H2O
TVKLQ + AGF-NH2
-
-
-
-
?
TVRLQAGF + H2O
TVRLQ + Ala-Gly-Phe
-
-
-
-
?
TVRLQSGF + H2O
TVRLQ + SGF
-
highest activity
-
-
?
TVTLQSGF-NH2 + H2O
TVTLQ + SGF-NH2
-
-
-
-
?
TVVLQSGF + H2O
TVVLQ + SGF
-
-
-
-
?
TVVLQSGF-NH2 + H2O
TVVLQ + SGF-NH2
-
-
-
-
?
VAVLQSGF + H2O
VAVLQ + SGF
-
-
-
-
?
VLQS-NH2 + H2O
VLQ + L-serinamide
-
-
-
-
?
VLQSG-NH2 + H2O
VLQ + Ser-Gly-NH2
-
-
-
-
?
VVRLQSGF + H2O
VVRLQ + SGF
-
-
-
-
?
VVTLQSGF-NH2 + H2O
VVTLQ + SGF-NH2
-
-
-
-
?
VVVLQSGF + H2O
VVVLQ + SGF
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-KNSTLQSGLRKE-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
?
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-KTSAVLQSGF RKME-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
?
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-KTSAVLQSGFRKME-5-['-(aminoethyl)amino]-naphthalenesulfonic acid + H2O
?
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-KTSAVLQSGFRKME-5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid + H2O
[4-(4-dimethylaminophenylazo)benzoic acid]-KTSAVLQ + SGFRKME-5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-KTSAVLQSGFRKME-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
?
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-VNSTLQSGLRK-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid]-M + H2O
?
-
-
-
-
?
additional information
?
-
coronavirus polyprotein + H2O
?
-
3CLpro processes the translated polyproteins to functional viral proteins
-
-
?
coronavirus polyprotein + H2O
?
during the formation of the coronaviral replication/transcription complex, essential steps include processing of the conserved polyprotein nsp7-10 region by the main protease Mpro and subsequent complex formation of the released nsps
-
-
?
coronavirus polyprotein + H2O
?
during the formation of the coronaviral replication/transcription complex, essential steps include processing of the conserved polyprotein nsp7-10 region by the main protease Mpro and subsequent complex formation of the released nsps. There is a clear order of cleavage efficiencies, which is influenced by the polyprotein tertiary structure. The predominant product is an nsp7+8(2:2) hetero-tetramer with nsp8 scaffold
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
DABCYL-TSAVLQSGFRKME-EDANS + H2O
DABCYL-TSAVLQ + SGFRKME-EDANS
internally quenched fluorescent peptide containing a consensus cleavage sequence, with DABCYL at the N-terminal and EDANS at the C-terminal end
-
-
?
DABCYL-TSAVLQSGFRKME-EDANS + H2O
DABCYL-TSAVLQ + SGFRKME-EDANS
internally quenched fluorescent peptide containing a consensus cleavage sequence, with DABCYL at the N-terminal and EDANS at the C-terminal end
-
-
?
H-Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-NH2 + H2O
H-Thr-Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys-NH2
-
-
-
?
H-Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-NH2 + H2O
H-Thr-Ser-Ala-Val-Leu-Gln + Ser-Gly-Phe-Arg-Lys-NH2
-
-
-
?
KVATVQSKMSD + H2O
KVATVQ + SKMSD
-
-
-
-
?
KVATVQSKMSD + H2O
KVATVQ + SKMSD
-
weak activity
-
-
?
NRATLQAIASE + H2O
NRATLQ + AIASE
-
-
-
-
?
NRATLQAIASE + H2O
NRATLQ + AIASE
-
weak activity
-
-
?
NVATLQAENVT + H2O
NVATLQ + AENVT
-
-
-
-
?
NVATLQAENVT + H2O
NVATLQ + AENVT
-
weak activity
-
-
?
REPLMQSADAS + H2O
REPLMQ + SADAS
-
-
-
-
?
REPLMQSADAS + H2O
REPLMQ + SADAS
-
weak activity
-
-
?
SARS-CoV Trx/GST-tagged C145A 3CLpro mutant + 2 H2O
Trx-10aa + C145A 3CLpro mutant + 10aa-GST
-
contains 2 x 10 additional amino acids for cleavage, substrate for 3CLpro processing by the wild-type 3CLpro, substrate is catalytically inactive
-
-
?
SARS-CoV Trx/GST-tagged C145A 3CLpro mutant + 2 H2O
Trx-10aa + C145A 3CLpro mutant + 10aa-GST
contains 2 x 10 additional amino acids for cleavage, substrate for 3CLpro processing by the wild-type 3CLpro, substrate is catalytically inactive
-
-
?
SARS-CoV-2 Trx/GST-tagged C145A 3CLpro mutant + 2 H2O
Trx-10aa + C145A 3CLpro mutant + 10aa-GST
-
contains 2 x 10 additional amino acids for cleavage, substrate for 3CLpro processing by the wild-type 3CLpro, substrate is catalytically inactive
-
-
?
SARS-CoV-2 Trx/GST-tagged C145A 3CLpro mutant + 2 H2O
Trx-10aa + C145A 3CLpro mutant + 10aa-GST
contains 2 x 10 additional amino acids for cleavage, substrate for 3CLpro processing by the wild-type 3CLpro, substrate is catalytically inactive
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SAVKLQNNELS + H2O
SAVKLQ + NNELS
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SAVKLQNNELS + H2O
SAVKLQ + NNELS
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weak activity
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SAVLQSGFRK + H2O
SAVLQ + SGFRK
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SAVLQSGFRK + H2O
SAVLQ + SGFRK
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best substrate for both, wild type and mutant enzyme T25G
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SGVTFQGKFKK + H2O
SGVTFQ + GKFKK
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SGVTFQGKFKK + H2O
SGVTFQ + GKFKK
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highest cleavage efficiency. The two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive ones
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TSAVLQSGFRK-NH2 + H2O
TSAVLQ + SGFRK-NH2
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TSAVLQSGFRK-NH2 + H2O
TSAVLQ + SGFRK-NH2
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highest cleavage efficiency. The two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive ones
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TSAVLQSGFRK-NH2 + H2O
TSAVLQ + SGFRK-NH2
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peptide containing the P1/P2 cleavage site, the N-terminal self-cleavage site of the protease, most suitable substrate
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additional information
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SARSCoV 3CLpro favors Ala and Ser, followed by Gly at the P1' position
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additional information
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the N-terminal cleavage site G-S of substrate is preferred over the C-terminal cleavage site Q-G
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a 3CLpro mechanism utilizes an electrostatic trigger to initiate the acylation reaction, a cysteine-histidine catalytic dyad ion pair, an enzyme-facilitated release of P1, and a general base catalyzed deacylation reaction
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additional information
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complete description of the tetrapeptide substrate specificity of 3Clpro using fully degenerate peptide libraries consisting of all 160 000 possible naturally occurring tetrapeptides. P1-Gln P2-Leu specificity and elucidate a novel preference for P1-His containing substrates equal to the expected preference for P1-Gln
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additional information
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SARS-CoV 3CLpro mediates extensive proteolytic processing of two overlapping replicase polyproteins, pp1a (486000 Da) and pp1ab (790000 Da), to yield the corresponding functional polypeptides that are essential for SARSCoV replication and transcription processes
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additional information
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the genomic RNA produces two large proteins with overlapping sequences, polyproteins 1a and 1ab, which are autocatalytically cleaved by two or three viral proteases to yield functional polypeptides. The key enzyme in this processing is SARS 3CL protease
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additional information
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a complete description of the tetrapeptide substrate specificity of 3Clpro using fully degenerate peptide libraries consisting of all 160000 possible naturally occurring tetrapeptides. The enzyme exhibits a strong preference for P1 Gln containing substrates and P2 Leu containing substrates. The enzyme also shows a strong preference for P1 histidine containing substrates. 3Clpro has extended substrate specificity at P5 and P6 preferring hydrophobic amino acids such as Leu
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additional information
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comprehensive overview of SARS-CoV 3CLpro substrate specificity. The hydrophobic pocket in the P2 position at the protease cleavage site is crucial to SARS-CoV 3CLpro-specific binding, which is limited to substitution by hydrophobic residue. The binding interface of SARS-CoV 3CLpro that is facing the P1' position is suggested to be occupied by acidic amino acids, thus the P1' position is intolerant to acidic residue substitution, owing to electrostatic repulsion. Steric hindrance caused by some bulky or branching amino acids in P3 and P2' positions may also hinder the binding of SARS-CoV 3CLpro. In addition to the conserved Gln residue in the P1 position at the SARS-CoV 3CLpro cleavage site, the P2 position, which is exclusively occupied by Leu residue, also serves as another important determinant of substrate specificity. Peptide substrate with Phe replacement in the P2 position is also favorable for SARSCoV 3CLpro cleavage. Ile is intolerant in the P2 position. P1' position, which is frequently occupied by Ser residue, also contributes to the substrate specificity of SARS-CoV 3CLpro considerably. The P1' position is highly unfavorable to the substitution by Pro, Asp, and Glu residues. The substrate specificity of SARS-CoV 3CLpro is less dependent on the P2' and P3 positions at the cleavage site. The peptide cleavage results show that the P3' and P4 positions have no effect on determining the substrate specificity preferences of SARS-CoV 3CLpro
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cuts the 11 peptides covering all of the 11 cleavage sites on the viral polyprotein with different efficiency
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the S3 subsite of the SARS CoVMpro has a negative character. The electrostatic interactions between Glu47 and P3Lys play a key role in specific binding. These observations are very important and provide further information for structural-based drug design against SARS virus
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3CLpro cleaves the replicase polyproteins at 11 sites with the conserved Gln-(Ser, Ala, Gly) sequences
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no cleavage of SAVLQPGFRK
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no activity towards SWTSAVKQSGFRKWA, SWTSAVRQSGFRKWA, SWTSAVEQSGFRKWA, and SWTSAVDQSGFRKWA
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no activity towards SWTSAVKQSGFRKWA, SWTSAVRQSGFRKWA, SWTSAVEQSGFRKWA, and SWTSAVDQSGFRKWA
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the substrate specificity of the enzyme requires glutamine in the P1 position and a large hydrophobic residue in the P2 position
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the substrate specificity of the enzyme requires glutamine in the P1 position and a large hydrophobic residue in the P2 position
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the enzyme performs autoprocessing, overview. As 3CLpro requires a glutamine residue at the P1 position of the substrate
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the enzyme shows a substrate-induced catalytic mechanism that further enhances its substrate specificity, overview
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