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EC unknown
Reaction Schemes
Broad substrate specificity with a preference for basic, aliphatic, and aromatic C-terminal amino acids. No activity with N-benzyloxycarbonyl-Ala-Asp, N-benzyloxycarbonyl-Ala-Asn, N-benzyloxycarbonyl-Ala-Pro, N-benzyloxycarbonyl-Ala-His.
Synonyms
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Broad substrate specificity with a preference for basic, aliphatic, and aromatic C-terminal amino acids. No activity with N-benzyloxycarbonyl-Ala-Asp, N-benzyloxycarbonyl-Ala-Asn, N-benzyloxycarbonyl-Ala-Pro, N-benzyloxycarbonyl-Ala-His.
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Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro + L-phenylalanine
Substrates: -
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + L-histidine
Substrates: -
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + L-leucine
Substrates: -
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + L-leucine
Substrates: -
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + L-valine
Substrates: -
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + L-tyrosine
Substrates: -
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + L-serine
Substrates: release of up to seven residues from the C-terminus
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N-benzyloxycarbonyl-Ala-Ala + H2O
N-benzyloxycarbonyl-Ala + L-alanine
Substrates: -
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N-benzyloxycarbonyl-Ala-Arg + H2O
N-benzyloxycarbonyl-Ala + L-arginine
Substrates: compared to the activity of Pyrococcus furiosus carboxypeptidase the catalytic efficiency is of Thermococcus onnurineus carboxypeptidase is 80-fold lower
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N-benzyloxycarbonyl-Ala-Leu + H2O
N-benzyloxycarbonyl-Ala + L-leucine
Substrates: -
?
N-benzyloxycarbonyl-Ala-Met + H2O
N-benzyloxycarbonyl-Ala + L-methionine
Substrates: -
?
N-benzyloxycarbonyl-Ala-Tyr + H2O
N-benzyloxycarbonyl-Ala + L-tyrosine
Substrates: -
?
N-benzyloxycarbonyl-Ala-Val + H2O
N-benzyloxycarbonyl-Ala + L-valine
Substrates: -
?
additional information
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Substrates: no activity with N-benzyloxycarbonyl-Ala-Asp, N-benzyloxycarbonyl-Ala-Asn, N-benzyloxycarbonyl-Ala-Pro, N-benzyloxycarbonyl-Ala-His
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Co2+
0.2 mM, stimulates activity, can not be replaced by other divalent metal ions, no activation by Zn2+
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Cu2+
0.2 mM, about 90% loss of activity, the inhibitory effect is not overcome by the presence of Co2+
EDTA
1 mM, complete inactivation
Fe2+
0.2 mM, about 70% loss of activity, the inhibitory effect is not overcome by the presence of Co2+
Ni2+
0.2 mM, about 75% loss of activity, the inhibitory effect is not overcome by the presence of Co2+
Zn2+
0.2 mM, about 90% loss of activity, the inhibitory effect is not overcome by the presence of Co2+
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1.4
N-benzyloxycarbonyl-Ala-Arg
pH 6.5, 70-80°C
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11.6
N-benzyloxycarbonyl-Ala-Arg
pH 6.5, 70-80°C
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8.3
N-benzyloxycarbonyl-Ala-Arg
pH 6.5, 70-80°C
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6.5
substrate: N-benzyloxycarbonyl-Ala-Arg
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5.3 - 7.5
pH 5.3: about 80% of maximal activity, pH 7.5: about 45% of maximal activity
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70 - 80
substrate: N-benzyloxycarbonyl-Ala-Arg
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50 - 90
50°C: about 50% of maximal activity, 90°C: about 60% of maximal activity
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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Q2QC89_9EURY
499
0
59198
TrEMBL
other Location (Reliability: 1 )
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61000
2 * 61000, SDS-PAGE
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dimer
2 * 61000, SDS-PAGE
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80
pH 6.5, 0.2 mM Co2+, t1/2: 84 min, t1/2 in absence of Co2+ is 7.4 min
90
pH 6.5, 0.2 mM Co2+, t1/2: 8 min, t1/2 in absence of Co2+ is 5 min
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Glycerol
12.5%, does not protect from inactivation at either temperature
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overexpression in Escherichia coli
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Lee, H.S.; Kim, Y.J.; Bae, S.S.; Jeon, J.H.; Lim, J.K.; Kang, S.G.; Lee, J.H.
Overexpression and characterization of a carboxypeptidase from the hyperthermophilic archaeon Thermococcus sp. NA1
Biosci. Biotechnol. Biochem.
70
1140-1147
2006
Thermococcus onnurineus (Q2QC89)
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