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Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
Ala-Ala-Ala-p-nitroanilide + H2O
Ala-Ala-Ala + p-nitroaniline
-
24% of the activity with Ala-Ala-Phe-p-nitroanilide
-
-
?
Ala-Ala-Phe 2-naphthylamide + H2O
Ala-Ala-Phe + 2-naphthylamine
-
at 41% the rate of Ala-Ala-Phe 7-amido-4-methylcoumarin
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Ala-Ala-Phe-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
angiotensin III + H2O
?
-
-
-
-
?
Arg-Ala-(dehydro)Ala-Val-Ala + H2O
?
-
inhibitor, at 0.05% the rate of Arg-Arg-Ala-(phospho)Ser-Val-Ala hydrolysis
-
-
?
Arg-Ala-Ser-Val-Ala + H2O
Arg-Ala-Ser + Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val + H2O
?
-
the Ala-(phospho)Ser bond is cleaved at the same rate as that of Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
Arg-Arg-Ala-Ser-Val + H2O
Arg-Arg-Ala + Ser-Val
-
-
-
-
?
Arg-Arg-Ala-Ser-Val-Ala + H2O
Arg-Arg-Ala + Ser-Val-Ala
-
better substrate than the phosphorylated peptide
-
-
?
Cholecystokinin + H2O
?
-
-
-
-
?
cholecystokinin octapeptide fragment + H2O
?
-
-
-
-
?
cholecystokinin-8-sulfate + H2O
Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2
-
-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O
Gly-Ser-His + Leu-Leu-Glu-Ala
Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Gly-Val-Leu + Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
major cleavage site: L-Arg, followed by cleavage at Ala-(phospho)Ser
-
?
Gly-Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Gly-Val-Leu + Arg-Arg-Ala-Ser-Val-Ala
-
-
-
-
?
His-Leu-His 2-naphthylamide + H2O
His-Leu-His + 2-naphthylamine
-
at 12% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
KKE-5-[(2-aminoethyl) amino]-naphthalene-1-sulfonic acid-Q9K-4'-dimethylaminoazobenzene-4'-sulfonyl + H2O
?
-
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
L-Ala-L-Ala-L-Phe-p-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + p-nitroaniline
-
-
-
?
L-Ala-L-Phe-L-Pro-p-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + p-nitroaniline
Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Leu-Arg-Arg + Ala-(phospho)Ser-Val-Ala
-
poor substrate
-
-
?
Leu-Leu-Glu-Ala + H2O
Leu-Leu-Glu + Ala
sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Lys-Arg-Ala-Ser-Val + H2O
Lys-Arg-Ala + Ser-Val
-
-
-
-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
neurokinin + H2O
?
-
-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
-
at 6% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
Pro-Pro-Ala-p-nitroanilide + H2O
Pro-Pro-Ala-p-nitroaniline
-
12% of the activity with Ala-Ala-Phe-p-nitroanilide
-
-
?
Q20RRGRR + H2O
Q17RRGRR + Q14RRGRR + QQQ
little activity
-
-
?
Val-Gly-Ala-His-Ala-Gly-Glu-Tyr-Gly-Ala-Glu-Ala-Leu-Glu-Arg + H2O
Val-Gly-Ala + His-Ala-Gly + Glu-Tyr-Gly + Ala-Glu-Ala + Leu-Glu-Arg
-
peptide derived from human hemoglobin alpha-chain, residues 17-31, sequential release of tripeptides from free N-terminus, cleaved into 5 tripeptides by human enzyme, cleavage of Gly25-Ala bond occurs at a lower rate than Ala19-His and Gly22-Glu
-
?
Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Val-Leu-Arg + Arg-Ala-Ser-Val-Ala
-
-
the latter product is cleaved at a higher rate than the substrate
?
Val-Tyr-Ser 2-naphthylamide + H2O
Val-Tyr-Ser + 2-naphthylamine
-
at 3% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
additional information
?
-
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
best chromogenic tripeptyl substrate
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Drosophila sp. (in: flies)
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
-
-
-
-
?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O
Gly-Ser-His + Leu-Leu-Glu-Ala
sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O
Gly-Ser-His + Leu-Leu-Glu-Ala
sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Phe-L-Pro-p-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + p-nitroaniline
-
-
-
-
?
L-Ala-L-Phe-L-Pro-p-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + p-nitroaniline
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide, aminoacyl or dipeptidyl methylcoumarylamides
-
-
?
additional information
?
-
-
no substrate: Pro-Lys-Ala 2-naphthylamide
-
-
?
additional information
?
-
-
no substrates are peptides with proline residues around cleavage sites
-
-
?
additional information
?
-
-
association/dissociation may be a way of regulating the enzyme activity in vivo
-
-
?
additional information
?
-
-
the enzyme is important for the degradation of some specific substrates, e.g. the neuropeptide cholecystokinin. It is likely that the main biological function of tripeptidyl-peptidase II is to participate in a general intracellular protein turnover. This peptidase may act on oligopeptides generated by the proteasome, or other endopeptidases, and the tripeptides formed would subsequently be good substrates for other exopeptidases. Tripeptidyl-peptidase II activity is increased in sepsis-induced muscle wasting, a situation of enhanced protein turnover
-
-
?
additional information
?
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
-
TPPII plays an important role in antigen processing, as most proteasomal products require further processing by TPPII for MHC class I presentation. As a consequence, peptide generation for MHCclass I is severely hampered when TPPII activitis inhibited
-
-
?
additional information
?
-
no activity against Q20RRGRR and KKQ30KK
-
-
?
additional information
?
-
-
tripeptidyl peptidase II plays a role in cross-presentation of CTL epitopes restricted to diverse HLA alleles
-
-
?
additional information
?
-
tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all
-
-
?
additional information
?
-
-
tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all
-
-
?
additional information
?
-
tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all
-
-
?
additional information
?
-
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
-
the activities of both the proteasome and PTTII are regulated in a parallel manner in cancer cachexia, and both are induced by the same factor and probably have the same intracellular signalling pathways and transcription factors
-
-
?
additional information
?
-
-
TPP II additionally has an endopeptidase activity and is able to attack longer disordered peptides up to 75 amino acid residues.Three cleavage sites after proline residues are noted, the endopeptidase activity is more promiscuous than expected, and certainly different from the specificity of the exopeptidase activity. No carboxypeptidase activity has been detected
-
-
?
additional information
?
-
-
PTP-A cleaves Xaa-Xaa-Pro-Yaa-(Xaa)n between Pro and Yaa, where Yaa represents any residue except proline, and Zaa represents any residue except glycine, proline, or a charged residue
-
-
?
additional information
?
-
-
PTP-A cleaves Xaa-Xaa-Pro-Yaa-(Xaa)n between Pro and Yaa, where Yaa represents any residue except proline, and Zaa represents any residue except glycine, proline, or a charged residue
-
-
?
additional information
?
-
-
requires free amino terminus
-
-
?
additional information
?
-
-
no substrate: Arg-Arg-Pro-Ser-Val
-
-
?
additional information
?
-
-
no substrates are Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala, guanidovaleric acid-Arg-Arg-Ala-(phospho)Ser-Val, guanidovaleric acid-Arg-Arg-Ala-Ser-Val, epsilon-aminohexanoic acid-Arg-Arg-Ala-Ser-Val
-
-
?
additional information
?
-
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
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(2S)-1-oxo-1-[(2S)-2-(5-propyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]butan-2-amine
-
IC50: 4 nM
(2S)-1-oxo-1-[(2S)-2-(5-propyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]propan-2-amine
-
IC50: 6 nM
(2S)-1-[(2S)-2-(5-ethyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]-1-oxopropan-2-amine
-
IC50: 23 nM
(2S)-2-[[(2S)-2-aminobutanoyl]amino]butanoic acid
-
-
(2S)-2-[[(2S)-2-aminobutanoyl]amino]pentanoic acid
-
-
(2S)-aminobutyryl-(4S)-fluoro-L-proline n-butylamide
-
-
(2S)-aminobutyryl-4-cis-benzyl-L-proline n-butylamide
-
-
(S)-valinyl-(S)-phenylalaninol amide
-
-
2,2'-Dithiopyridine
-
strong
2-(2-amino-3-methyl-butyrylamino)-4-phenyl-butyric acid
-
-
2-amino-1-[2-(4-propyl-1H-imidazol-2-yl)-2,3-dihydroindol-1-yl]ethanone
-
IC50: 36 nM
2-amino-3-methyl-N-(3-phenyl-propyl)-butyramide
-
-
2-amino-3-methyl-N-phenethyl-butyramide
-
-
2-amino-N-benzyl-3-methyl-butyramide
-
-
3,4-dichloroisocoumarin
-
-
Acetyl-Val-Leu-Leu-Arg-Ala-Ser-Val-Ala
-
weak
Ala-Ala-Phe-chloromethyl ketone
Ala-Ala-Phe-chloromethylketone
aminobutyryl-L-Pro-n-butylamide
-
-
aminobutyryl-Phe-n-butylamide
-
-
aminobutyryl-Pro-n-butylamide
-
-
Arg-Ala-(dehydro)Ala-Val-Ala
-
-
Arg-Ala-(phospho)Ser-Val-Ala
-
-
Arg-Ala-DELTAAla-Val-Ala
-
competitive
Arg-Arg-Ala-(dehydro)Ala-Val-Ala
-
less effective than Arg-Ala-(dehydro)Ala-Val-Ala
Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
inhibits cleavage of Leu-Arg bond, Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala as substrate
butabindide oxalate
-
specific TPPII inhibitor
butyloxycarbonyl-Val-Nle-OH
-
-
Diazoacetyl norleucine methyl ester
-
weak
diisopropyl fluorophosphate
diphenyl [1-([1-[(2S)-2-aminobutanoyl]-2,3-dihydro-1H-indole-2-carbonyl]amino)-3-methylbutyl]phosphonate
irreversible variant of butabindide. almost 60fold more potent than butabindide
Guanidinovaleric acid-Arg-Ala-(phospho)Ser-Val
-
-
Hg2+
-
strong, reversible by dialysis against 2 mM DTT
isovaleryl-L-Leu-L-Arg-L-Arg-L-Ala-L-Ser-L-Val-L-Ala
-
L-Ala-L-Ala-L-Phe-chloromethane
-
-
L-Ala-L-Ala-L-Phe-chloromethylketone
-
-
L-Val-L-Leu-L-Arg-L-Arg-L-Ala-L-Ser-L-Val-L-Ala
-
Leu-Arg-Arg-Ala-(phospho)Ser-Val
-
weak, Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala as substrate
Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
weak, Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala as substrate
N-[[(L-arginyl-L-alanyl)amino](oxo)acetyl]-L-valyl-L-alanine
-
potent inhibitor
PhCH2OCO-Val-Nle-O(CH2)3CH3
-
-
Soybean trypsin inhibitor
-
weak
-
trans-epoxysuccinyl-L-leucinamido(4-guanidino)butane
-
i.e. E-64, weak
Val-(beta-naphthyl)Ala-OH
-
-
Val-(S)-cyclohexylalanyl-NH(CH2)3CH3
-
-
Val-(S)-cyclohexylalanyl-OH
-
-
Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
hydrolysis of Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala
Val-phenylglycine-NHCH3
-
-
Ala-Ala-Phe-chloromethyl ketone
-
0.03 mM
Ala-Ala-Phe-chloromethyl ketone
-
0.02 mM
Ala-Ala-Phe-chloromethylketone
-
-
Ala-Ala-Phe-chloromethylketone
-
-
Ala-Ala-Phe-chloromethylketone
-
-
butabindide
-
50% inhibition at 0.005 mM, more than 97% inhibition at 0.1 mM
butabindide
-
0.002 mM, 83% inhibition
butabindide
-
competitive
butabindide
specific TPPII inhibitor
butabindide
-
specific inhibitor
butabindide
efficient, competitive inhibitor of TPP II
butabindide
-
a potent reversible competitive and selective inhibitor
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
strong, Val-Leu-Leu-Arg-Ala-Ser-Val-Ala protects
NEM
-
1 mM, 87% inhibition
PCMB
-
0.2 mM, 97% inhibition
PMSF
-
1 mM nearly complete inactivation
PMSF
-
strong, irreversible, Val-Leu-Leu-Arg-Ala-Ser-Val-Ala protects
additional information
-
insensitive to NEM, MG132 and lactacystin
-
additional information
-
no inhibition by Val-Leu-Arg, isovaleryl-Val-Leu-Arg-Arg-Ala-Ser-Val-Ala, EDTA (with or without DTT)
-
additional information
-
no inhibition by bestatin
-
additional information
no or poor inhibition by Streptomyces subtilisin inhibitor (SSI), API-2, 4-chloromercuribenzoate, 2,2'-dithiodipyridine, iodoacetate, talopeptin, Streptomyces pepsin inhibitor (S-PI), amastatin, bestatin, and arphamenine A
-
additional information
-
no or poor inhibition by Streptomyces subtilisin inhibitor (SSI), API-2, 4-chloromercuribenzoate, 2,2'-dithiodipyridine, iodoacetate, talopeptin, Streptomyces pepsin inhibitor (S-PI), amastatin, bestatin, and arphamenine A
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0036 - 0.13
Ala-Ala-Ala-4-nitroanilide
0.016
Ala-Ala-Phe 4-methylcoumarin 7-amide
-
-
0.012 - 0.88
Ala-Ala-Phe-4-nitroanilide
0.11 - 0.47
Ala-Ala-Phe-7-amido-4-methylcoumarin
0.02
Ala-Ala-Phe-p-nitroanilide
-
pH 7.5, 37°C
0.008 - 0.015
Arg-Arg-Ala-(phospho)Ser-Val-Ala
0.008 - 20
L-Ala-L-Ala-L-Ala 4-nitroanilide
0.017 - 30
L-Ala-L-Ala-L-Phe 4-nitroanilide
0.013 - 1
L-Ala-L-Ala-L-Phe-p-nitroanilide
0.0036
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
0.008
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
0.009
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
0.01
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
0.01
Ala-Ala-Ala-4-nitroanilide
-
pH 7.6, 37°C
0.01
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
0.01
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.012
Ala-Ala-Ala-4-nitroanilide
-
pH 6.8, 37°C
0.013
Ala-Ala-Ala-4-nitroanilide
-
pH 6.4, 37°C
0.013
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.014
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
0.015
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
0.017
Ala-Ala-Ala-4-nitroanilide
-
pH 7.9, 37°C
0.024
Ala-Ala-Ala-4-nitroanilide
-
pH 8.3, 37°C
0.03
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
0.039
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant D387G
0.05
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.05
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant D387G
0.05
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.054
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.057
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.06
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant D387G
0.06
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant D387G
0.062
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.13
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.012
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
0.012
Ala-Ala-Phe-4-nitroanilide
-
pH 8.3, 37°C
0.017
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
0.024
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
0.028
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
0.03
Ala-Ala-Phe-4-nitroanilide
-
pH 6.8, 37°C
0.037
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.042
Ala-Ala-Phe-4-nitroanilide
-
pH 6.4, 37°C
0.05
Ala-Ala-Phe-4-nitroanilide
-
pH 7.6, 37°C
0.054
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
0.056
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.058
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
0.06
Ala-Ala-Phe-4-nitroanilide
-
pH 7.9, 37°C
0.062
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.07
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.074
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.09
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
0.09
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.1
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.11
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.2
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant D387G
0.21
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
0.25
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant D387G
0.27
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant D387G
0.33
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant D387G
0.88
Ala-Ala-Phe-4-nitroanilide
pH 7.5, 37°C, recombinant enzyme
0.11
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
0.44
Ala-Ala-Phe-7-amido-4-methylcoumarin
Drosophila sp. (in: flies)
-
pH 7.5, 30°C, recombinant enzyme
0.47
Ala-Ala-Phe-7-amido-4-methylcoumarin
Drosophila sp. (in: flies)
-
pH 7.5, 30°C, native enzyme
0.008
Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
pH 6.5
0.013
Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
-
0.015
Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
pH 7.5
0.008
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.6, 37°C
0.009
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.01
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
0.01
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.01
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.9, 37°C
0.0106
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 7.6, 37°C
0.012
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 6.8, 37°C
0.013
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 6.4, 37°C
0.013
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
0.014
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 8.3, 37°C
0.015
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
0.017
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 7.9, 37°C
0.024
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 8.3, 37°C
0.03
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
0.036
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
0.039
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.6, 37°C
0.05
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
0.05
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
0.05
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.8, 37°C
0.054
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
0.057
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
0.06
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.4, 37°C
0.06
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.9, 37°C
0.062
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
0.13
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 8.3, 37°C
0.6
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
1.19
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
3.3
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
5
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
20
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
0.017
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.024
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.028
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.6, 37°C
0.03
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 6.8, 37°C
0.037
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.9, 37°C
0.042
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 6.4, 37°C
0.05
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 7.6, 37°C
0.054
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 8.3, 37°C
0.056
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
0.058
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
0.06
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 7.9, 37°C
0.062
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
0.07
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
0.074
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
0.09
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
0.09
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
0.1
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
0.11
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 8.3, 37°C
0.12
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 8.3, 37°C
0.12
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
0.2
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.4, 37°C
0.21
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
0.25
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.6, 37°C
0.27
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.9, 37°C
0.3
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.8, 37°C
0.5
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
0.6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
0.9
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
30
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
0.013
L-Ala-L-Ala-L-Phe-p-nitroanilide
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
1
L-Ala-L-Ala-L-Phe-p-nitroanilide
mutant enzyme E331K, Km above 1.0 mM, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
1
L-Ala-L-Ala-L-Phe-p-nitroanilide
mutant enzyme E331Q, Km above 1.0 mM, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.25 - 33
Ala-Ala-Ala-4-nitroanilide
0.38 - 114
Ala-Ala-Phe-4-nitroanilide
0.25 - 100
L-Ala-L-Ala-L-Ala 4-nitroanilide
0.38 - 500
L-Ala-L-Ala-L-Phe 4-nitroanilide
0.25
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.509
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.58
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.74
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.857
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant H267A
1.12
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant H267A
1.29
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant D387G
1.3
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant D387G
1.42
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant D387G
1.5
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant D387G
2
Ala-Ala-Ala-4-nitroanilide
-
pH 6.4, 37°C
3.1
Ala-Ala-Ala-4-nitroanilide
-
pH 7.6, 37°C
3.3
Ala-Ala-Ala-4-nitroanilide
-
pH 8.3, 37°C
4
Ala-Ala-Ala-4-nitroanilide
-
pH 6.8, 37°C
5
Ala-Ala-Ala-4-nitroanilide
-
pH 7.9, 37°C
11
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
12
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
12
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
13
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
13
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
21
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
27
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
30
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
33
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
33
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.38
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.441
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.86
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.9
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.9
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant H267A
1
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant D387G
3
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant D387G
5
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant D387G
6
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant D387G
7.2
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant D387G
9.6
Ala-Ala-Phe-4-nitroanilide
-
pH 6.4, 37°C
10
Ala-Ala-Phe-4-nitroanilide
-
pH 6.8, 37°C
19
Ala-Ala-Phe-4-nitroanilide
-
pH 7.9, 37°C
21
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
22
Ala-Ala-Phe-4-nitroanilide
-
pH 7.6, 37°C
27
Ala-Ala-Phe-4-nitroanilide
-
pH 8.3, 37°C
38
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
42
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
43
Ala-Ala-Phe-4-nitroanilide
pH 7.5, 37°C, recombinant enzyme
50
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
56.8
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
57
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
60
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
65
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
96
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
114
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.25
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.509
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.58
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.6, 37°C
0.74
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 8.3, 37°C
0.857
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 8.3, 37°C
1.12
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.9, 37°C
1.29
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.9, 37°C
1.3
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.4, 37°C
1.42
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.6, 37°C
1.5
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.8, 37°C
2
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 6.4, 37°C
3.1
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 7.6, 37°C
3.3
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 8.3, 37°C
4
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 6.8, 37°C
4.2
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
5
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 7.9, 37°C
10
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
10
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
11
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
11
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
12
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
12
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
13
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
13
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
21
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
27
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
30
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
33
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
33
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
100
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
0.38
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.441
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 8.3, 37°C
0.86
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.9, 37°C
0.9
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.9
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.6, 37°C
1
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 8.3, 37°C
3
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.9, 37°C
4
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
4
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
5
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.4, 37°C
6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.6, 37°C
7.2
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.8, 37°C
9.6
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 6.4, 37°C
10
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 6.8, 37°C
18
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
19
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 7.9, 37°C
22
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 7.6, 37°C
27
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 8.3, 37°C
38
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
42
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
50
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
57
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
58.8
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
60
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
65
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
80
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
96
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
114
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
125
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
500
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000005 - 0.0039
Ala-Ala-Ala-4-nitroanilide
0.0000038 - 48.9
Ala-Ala-Phe-4-nitroanilide
3.4 - 3900
L-Ala-L-Ala-L-Ala 4-nitroanilide
3.82 - 3500
L-Ala-L-Ala-L-Phe 4-nitroanilide
0.000005
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.000006
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.00001
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.000011
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.000014
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.00002
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.000021
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant D387G
0.000021
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant D387G
0.00003
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant D387G
0.000036
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant D387G
0.000138
Ala-Ala-Ala-4-nitroanilide
-
pH 6.4, 37°C
0.00016
Ala-Ala-Ala-4-nitroanilide
-
pH 8.3, 37°C
0.00023
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
0.00028
Ala-Ala-Ala-4-nitroanilide
-
pH 7.6, 37°C
0.0003
Ala-Ala-Ala-4-nitroanilide
-
pH 7.9, 37°C
0.0003
Ala-Ala-Ala-4-nitroanilide
-
pH 6.8, 37°C
0.00033
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
0.0005
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
0.0009
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
0.001
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.0015
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
0.0026
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.0029
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
0.0038
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
0.0039
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
0.0000038
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.000006
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.000007
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.00001
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.000012
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant D387G
0.000013
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.0000165
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.000022
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant D387G
0.000023
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant D387G
0.00003
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant D387G
0.00019
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
0.00023
Ala-Ala-Phe-4-nitroanilide
-
pH 6.4, 37°C
0.00025
Ala-Ala-Phe-4-nitroanilide
-
pH 8.3, 37°C
0.00031
Ala-Ala-Phe-4-nitroanilide
-
pH 6.8, 37°C
0.00033
Ala-Ala-Phe-4-nitroanilide
-
pH 7.9, 37°C
0.00037
Ala-Ala-Phe-4-nitroanilide
-
pH 7.6, 37°C
0.00056
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
0.00056
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
0.00082
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.00098
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
0.0018
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
0.0025
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
0.0028
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
0.0031
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.0035
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
48.9
Ala-Ala-Phe-4-nitroanilide
pH 7.5, 37°C, recombinant enzyme
3.4
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
5
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.4, 37°C
6
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 8.3, 37°C
6.7
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
8
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
9
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
9.6
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
10
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.8, 37°C
11
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.6, 37°C
14
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 8.3, 37°C
20
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.9, 37°C
21
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.4, 37°C
21
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.9, 37°C
30
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.8, 37°C
36
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.6, 37°C
138
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 6.4, 37°C
160
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 8.3, 37°C
280
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 7.6, 37°C
300
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 7.9, 37°C
300
L-Ala-L-Ala-L-Ala 4-nitroanilide
-
pH 6.8, 37°C
330
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
500
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
900
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
1000
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
1500
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
2100
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
2600
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
2900
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
3800
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
3900
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
3.82
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.4, 37°C
6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 8.3, 37°C
6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
7.1
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 8.3, 37°C
10
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.9, 37°C
12
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.9, 37°C
13
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.8, 37°C
15
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
15
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
16.5
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.6, 37°C
17
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
20
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
22
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.8, 37°C
23
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.6, 37°C
30
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.4, 37°C
190
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
230
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 6.4, 37°C
250
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 8.3, 37°C
310
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 6.8, 37°C
330
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 7.9, 37°C
370
L-Ala-L-Ala-L-Phe 4-nitroanilide
-
pH 7.6, 37°C
560
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
560
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
820
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
980
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
1800
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
2500
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
2800
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
3100
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
3500
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Balw, R.M.; Ragnarsson, U.; Zetterquist, .
Tripeptidyl aminopeptidase in the extralysosomal fraction of rat liver
J. Biol. Chem.
258
11622-11628
1983
Rattus norvegicus
brenda
Tomkinson, B.; Wernstedt, C.; Hellman, U.; Zetterquist, .
Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type
Proc. Natl. Acad. Sci. USA
84
7508-7512
1987
Homo sapiens
brenda
Balw, R.M.; Tomkinson, B.; Ragnarsson, U.; Zetterquist, .
Purification, substrate specificity, and classification of tripeptidyl peptidase II
J. Biol. Chem.
261
2409-2417
1986
Homo sapiens, Rattus norvegicus
brenda
Macpherson, E.; Tomkinson, B.; Balw, R.M.; Hglund, S.; Zetterquist, .
Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity
Biochem. J.
248
259-263
1987
Homo sapiens
brenda
Balw, R.M.; Eriksson, I.
Tripeptidyl peptidase II in haemolysates and liver homogenates of various species
Biochem. J.
241
75-80
1987
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Platyrrhini, no activity in Escherichia coli, Rattus norvegicus, Sus scrofa
brenda
Tomkinson, B.; Zetterquist, .
Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin
Biochem. J.
267
149-154
1990
Homo sapiens
brenda
Tomkinson, B.; Grehn, L.; Fransson, B.; Zetterquist, ?.
Use of a dehydroalanine-containing peptide as an efficient inhibitor of tripeptidyl peptidase II
Arch. Biochem. Biophys.
314
276-279
1994
Homo sapiens
brenda
Tomkinson, B.; Nyberg, F.
Distribution of tripeptidyl-peptidase II in the central nervous system of rat
Neurochem. Res.
20
1443-1447
1995
Rattus norvegicus
brenda
Matrinsson, T.; Vujic, M.; Tomkinson, B.
Localization of the human tripeptidyl peptidase II gene (TPP2) to 13q32-q33 by nonradioactive in situ hybridization and somatic cell hybrids
Genomics
17
493-495
1993
Homo sapiens
brenda
Wilson, C.; Gibosn, A.M.; McDermott, J.R.
Purification and characterization of tripeptidylpeptidase-II from post-mortem human brain
Neurochem. Res.
18
743-749
1993
Homo sapiens
brenda
Tomkinson, B.
Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II
Biomed. Biochim. Acta
50
727-729
1991
Homo sapiens
brenda
Harris, J.; Tomkinson, B.
Electron microscopical and biochemical studies on the oligomeric states of human erythrocyte tripeptidyl peptidase-II
Micron Microsc. Acta
21
77-89
1990
Homo sapiens
-
brenda
Tomkinson, B.
Characterization of cDNA for murine tripeptidyl-peptidase II reveals alternative splicing [published erratum appears in Biochem J 1995 Mar 15;306(Pt 3):880]
Biochem. J.
304
517-523
1994
Mus musculus
brenda
Tomkinson, B.
Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity
Arch. Biochem. Biophys.
376
275-280
2000
Homo sapiens
brenda
Tomkinson, B.; Ni Laoi, B.; Wellington, K.
The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex
Eur. J. Biochem.
269
1438-1443
2002
Homo sapiens, Mus musculus
brenda
Tomkinson, B.; Hansen, M.; Cheung, W.F.
Structure-function studies of recombinant murine tripeptidyl-peptidase II: the extra domain which is subject to alternative splicing is involved in complex formation
FEBS Lett.
405
277-280
1997
Mus musculus
brenda
Renn, S.C.; Tomkinson, B.; Taghert, P.H.
Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster
J. Biol. Chem.
273
19173-19182
1998
Drosophila melanogaster, Rattus norvegicus
brenda
Ganellin, C.R.; Bishop, P.B.; Bambal, R.B.; Chan, S.M.; Law, J.K.; Marabout, B.; Luthra, P.M.; Moore, A.N.; Peschard, O.; Bourgeat, P.; Rose, C.; Vargas, F.; Schwartz, J.C.
Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors
J. Med. Chem.
43
664-674
2000
Rattus norvegicus
brenda
Breslin, H.J.; Miskowski, T.A.; Kukla, M.J.; Leister, W.H.; De Winter, H.L.; Gauthier, D.A.; Somers, M.V.; Peeters, D.C.; Roevens, P.W.
Design, synthesis, and tripeptidyl peptidase II inhibitory activity of a novel series of (S)-2,3-dihydro-2-(4-alkyl-1H-imidazol-2-yl)-1H-indoles
J. Med. Chem.
45
5303-5310
2002
Rattus norvegicus
brenda
Hilbi, H.; Jozsa, E.; Tomkinson, B.
Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis
Biochim. Biophys. Acta
1601
149-154
2002
Homo sapiens
brenda
Radu, D.; Tomkinson, B.; Zachrisson, O.; Weber, G.; de Belleroche, J.; Hirsch, S.; Lindefors, N.
Overlapping regional distribution of CCK and TPPII mRNAs in Cynomolgus monkey brain and correlated levels in human cerebral cortex (BA 10)
Brain Res.
1104
175-182
2006
Macaca fascicularis, Rattus norvegicus, Homo sapiens (P29144)
brenda
Chand, A.; Wyke, S.M.; Tisdale, M.J.
Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle
Cancer Lett.
218
215-222
2005
Mus musculus
brenda
Lindas, A.C.; Tomkinson, B.
Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II
Gene
345
249-257
2005
Homo sapiens
brenda
Reits, E.; Neijssen, J.; Herberts, C.; Benckhuijsen, W.; Janssen, L.; Drijfhout, J.W.; Neefjes, J.
A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
Immunity
20
495-506
2004
Homo sapiens
brenda
Tomkinson, B.; Lindas, A.C.
Tripeptidyl-peptidase II: a multi-purpose peptidase
Int. J. Biochem. Cell Biol.
37
1933-1937
2005
Homo sapiens
brenda
Seyit, G.; Rockel, B.; Baumeister, W.; Peters, J.
Size matters: the spindle form of the 6 MDA tripeptidylpeptidase II from drosophila melanogaster stabilizes the activated state
J. Biol. Chem.
281
25723-25733
2006
Drosophila sp. (in: flies)
brenda
Ganellin, C.R.; Bishop, P.B.; Bambal, R.B.; Chan, S.M.; Leblond, B.; Moore, A.N.; Zhao, L.; Bourgeat, P.; Rose, C.; Vargas, F.; Schwartz, J.C.
Inhibitors of tripeptidyl peptidase II. 3. Derivation of butabindide by successive structure optimizations leading to a potential general approach to designing exopeptidase inhibitors
J. Med. Chem.
48
7333-7342
2005
Rattus norvegicus
brenda
Book, A.J.; Yang, P.; Scalf, M.; Smith, L.M.; Vierstra, R.D.
Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis
Plant Physiol.
138
1046-1057
2005
Arabidopsis sp.
brenda
Rockel, B.; Peters, J.; Mueller, S.A.; Seyit, G.; Ringler, P.; Hegerl, R.; Glaeser, R.M.; Baumeister, W.
Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II
Proc. Natl. Acad. Sci. USA
102
10135-10140
2005
Drosophila sp. (in: flies)
brenda
Naujokat, C.; Fuchs, D.; Berges, C.
Adaptive modification and flexibility of the proteasome system in response to proteasome inhibition
Biochim. Biophys. Acta
1773
1389-1397
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Levengood, M.R.; van der Donk, W.A.
Use of lantibiotic synthetases for the preparation of bioactive constrained peptides
Bioorg. Med. Chem. Lett.
18
3025-3028
2008
Homo sapiens
brenda
Hong, X.; Lei, L.; Kuenert, B.; Naredla, R.; Applequist, S.E.; Grandien, A.; Glas, R.
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors
Cancer Res.
67
7165-7174
2007
Homo sapiens
brenda
Bhutani, N.; Venkatraman, P.; Goldberg, A.L.
Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
EMBO J.
26
1385-1396
2007
Homo sapiens (P29144)
brenda
Basler, M.; Groettrup, M.
No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes
Eur. J. Immunol.
37
896-904
2007
Homo sapiens
brenda
Endert, P.
Role of tripeptidyl peptidase II in MHC class I antigen processing - the end of controversies?
Eur. J. Immunol.
38
609-613
2008
Homo sapiens
brenda
Marcilla, M.; Villasevil, E.M.; de Castro, J.A.
Tripeptidyl peptidase II is dispensable for the generation of both proteasome-dependent and proteasome-independent ligands of HLA-B27 and other class I molecules
Eur. J. Immunol.
38
631-639
2008
Homo sapiens
brenda
Lindas, A.C.; Tomkinson, B.
Characterization of the promoter of the gene encoding human tripeptidyl-peptidase II and identification of upstream silencer elements
Gene
393
62-69
2007
Homo sapiens
brenda
Preuss, K.D.; Held, G.; Kubuschok, B.; Hung, C.Z.; Malatsidze, N.; Wagner, M.; Pfreundschuh, M.
Identification of antigenic targets of paraproteins by expression cloning does not support a causal role of chronic antigenic stimulation in the pathogenesis of multiple myeloma and MGUS
Int. J. Cancer
121
459-461
2007
Homo sapiens
brenda
Guil, S.; Rodriguez-Castro, M.; Aguilar, F.; Villasevil, E.M.; Anton, L.C.; Del Val, M.
Need for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimental
J. Biol. Chem.
281
39925-39934
2006
Homo sapiens
brenda
Huai, J.; Firat, E.; Nil, A.; Million, D.; Gaedicke, S.; Kanzler, B.; Freudenberg, M.; van Endert, P.; Kohler, G.; Pahl, H.L.; Aichele, P.; Eichmann, K.; Niedermann, G.
Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice
Proc. Natl. Acad. Sci. USA
105
5177-5182
2008
Mus musculus
brenda
Anton, L.C.; Villasevil, E.M.
Is there an alternative to the proteasome in cytosolic protein degradation?
Biochem. Soc. Trans.
36
839-842
2008
Homo sapiens
brenda
Lindas, A.C.; Eriksson, S.; Jozsa, E.; Tomkinson, B.
Investigation of a role for Glu-331 and Glu-305 in substrate binding of tripeptidyl-peptidase II
Biochim. Biophys. Acta
1784
1899-1907
2008
Mus musculus (Q64514)
brenda
Firat, E.; Tsurumi, C.; Gaedicke, S.; Huai, J.; Niedermann, G.
Tripeptidyl peptidase II plays a role in the radiation response of selected primary cell types but not based on nuclear translocation and p53 Sstabilization
Cancer Res.
69
3325-3331
2009
Mus musculus
brenda
Tye, C.E.; Lorenz, R.L.; Bartlett, J.D.
Lysosomal protease expression in mature enamel
Cells Tissues Organs
189
111-114
2009
Mus musculus
brenda
Schnurr, M.; Orban, M.; Robson, N.C.; Shin, A.; Braley, H.; Airey, D.; Cebon, J.; Maraskovsky, E.; Endres, S.
ISCOMATRIX adjuvant induces efficient cross-presentation of tumor antigen by dendritic cells via rapid cytosolic antigen delivery and processing via tripeptidyl peptidase II
J. Immunol.
182
1253-1259
2009
Homo sapiens
brenda
Oda, H.; Saiki, K.; Tonosaki, M.; Yajima, A.; Konishi, K.
Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis
J. Periodont. Res.
44
362-267
2008
Porphyromonas gingivalis, Porphyromonas gingivalis W83
brenda
Tsurumi, C.; Firat, E.; Gaedicke, S.; Huai, J.; Mandal, P.K.; Niedermann, G.
Viability and DNA damage responses of TPPII-deficient Myc- and Ras-transformed fibroblasts
Biochem. Biophys. Res. Commun.
386
563-568
2009
Mus musculus (Q64514)
brenda
Grauling-Halama, S.; Bahr, U.; Schenk, S.; Geginat, G.
Role of tripeptidyl peptidase II in the processing of Listeria monocytogenes-derived MHC class I-presented antigenic peptides
Microbes Infect.
11
795-802
2009
Mus musculus
brenda
Nahalkova, J.; Tomkinson, B.
TPPII, MYBBP1A and CDK2 form a protein-protein interaction network
Arch. Biochem. Biophys.
564
128-135
2014
Homo sapiens
brenda
Eklund, S.; Dogan, J.; Jemth, P.; Kalbacher, H.; Tomkinson, B.
Characterization of the endopeptidase activity of tripeptidyl-peptidase II
Biochem. Biophys. Res. Commun.
424
503-507
2012
Mus musculus
brenda
Eklund, S.; Lindas, A.C.; Hamnevik, E.; Widersten, M.; Tomkinson, B.
Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics
Biochim. Biophys. Acta
1824
561-570
2012
Drosophila melanogaster, Drosophila melanogaster (Q9V6K1), Homo sapiens, Mus musculus, Mus musculus (Q64514)
brenda
Usukura, K.; Kasamatsu, A.; Okamoto, A.; Kouzu, Y.; Higo, M.; Koike, H.; Sakamoto, Y.; Ogawara, K.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Tripeptidyl peptidase II in human oral squamous cell carcinoma
J. Cancer Res. Clin. Oncol.
139
123-130
2013
Homo sapiens, Homo sapiens (P29144)
brenda
Zhou, Y.; Ru, Y.; Wang, C.; Wang, S.; Zhou, Z.; Zhang, Y.
Tripeptidyl peptidase II regulates sperm function by modulating intracellular Ca(2+) stores via the ryanodine receptor
PLoS ONE
8
e66634
2013
Mus musculus, Mus musculus (Q64514)
brenda
Schoenegge, A.M.; Villa, E.; Foerster, F.; Hegerl, R.; Peters, J.; Baumeister, W.; Rockel, B.
The structure of human tripeptidyl peptidase II as determined by a hybrid approach
Structure
20
593-603
2012
Homo sapiens (P29144), Homo sapiens
brenda
Ekino, K.; Yonei, S.; Oyama, H.; Oka, T.; Nomura, Y.; Shin, T.
Cloning, purification, and characterization of tripeptidyl peptidase from Streptomyces herbaricolor TY-21
Appl. Biochem. Biotechnol.
184
239-252
2018
Kitasatospora herbaricolor (D1MVE1), Kitasatospora herbaricolor, Kitasatospora herbaricolor TY-21 (D1MVE1)
brenda
Bialy, L.P.; Kuckelkorn, U.; Henklein, P.; Fayet, J.; Wilczynski, G.M.; Kaminski, A.; Mlynarczuk-Bialy, I.
Changes in spatio-temporal localization of tripeptidyl peptidase II (TPPII) in murine colon adenocarcinoma cells during aggresome formation a microscopy study based on a novel fluorescent proteasome inhibitor
Histol. Histopathol.
34
359-372
2019
Mus musculus
brenda
Wiemhoefer, A.; Stargardt, A.; van der Linden, W.A.; Renner, M.C.; van Kesteren, R.E.; Stap, J.; Raspe, M.A.; Tomkinson, B.; Kessels, H.W.; Ovaa, H.; Overkleeft, H.S.; Florea, B.; Reits, E.A.
Tripeptidyl peptidase II mediates levels of nuclear phosphorylated ERK1 and ERK2
Mol. Cell. Proteomics
14
2177-2193
2015
Homo sapiens (P29144)
brenda
Fukuda, Y.; Beck, F.; Plitzko, J.M.; Baumeister, W.
In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes
Proc. Natl. Acad. Sci. USA
114
4412-4417
2017
Rattus norvegicus (Q64560)
brenda