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EC Tree
The expected taxonomic range for this enzyme is: Pyrococcus furiosus
Reaction Schemes
broad specificity for neutral, aromatic, polar, and basic C-terminal residues. No activity with N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Glu.
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broad specificity for neutral, aromatic, polar, and basic C-terminal residues. No activity with N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Glu.
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Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro + L-phenylalanine
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Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + L-histidine
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Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + L-leucine
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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
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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
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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
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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
stepwise hydrolysis of up to seven residues from the C-terminus
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N-carboxybenzoyl-Ala-Ala + H2O
N-carboxybenzoyl-Ala + L-alanine
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N-carboxybenzoyl-Ala-Arg + H2O
N-carboxybenzoyl-Ala + L-arginine
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N-carboxybenzoyl-Ala-Ile + H2O
N-carboxybenzoyl-Ala + L-isoleucine
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N-carboxybenzoyl-Ala-Leu + H2O
N-carboxybenzoyl-Ala + L-leucine
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N-carboxybenzoyl-Ala-Lys + H2O
N-carboxybenzoyl-Ala + L-lysine
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N-carboxybenzoyl-Ala-Met + H2O
N-carboxybenzoyl-Ala + L-methionine
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N-carboxybenzoyl-Ala-Phe + H2O
N-carboxybenzoyl-Ala + L-phenylalanine
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N-carboxybenzoyl-Ala-Trp + H2O
N-carboxybenzoyl-Ala + L-tryptophan
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N-carboxybenzoyl-Ala-Tyr + H2O
N-carboxybenzoyl-Ala + L-tyrosine
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N-carboxybenzoyl-Ala-Val + H2O
N-carboxybenzoyl-Ala + L-valine
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additional information
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additional information
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the enzyme is involved in digestion and protein turnover
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additional information
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the enzyme is involved in digestion and protein turnover
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additional information
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no activity with N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Glu
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additional information
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no activity with N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Glu
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additional information
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additional information
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the enzyme is involved in digestion and protein turnover
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additional information
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the enzyme is involved in digestion and protein turnover
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
purified in its inactive state by the addition of EDTA and dithiothreitol to purification buffers, and the activity is restored by the addition of Co2+. No activation by Zn2+
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DTT
2 mM, complete inhibition
EDTA
1 mM, complete inhibition. Inhibition is fully reversible upon 50fold dilution and re-activation by Co2+
additional information
the serine protease inhibitor phenylmethylsulfonyl fluoride has no effect on the activity
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additional information
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the serine protease inhibitor phenylmethylsulfonyl fluoride has no effect on the activity
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0.9
N-carboxybenzoyl-Ala-Arg
80°C, pH 6.5, 0.4 mM CoCl2
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600
N-carboxybenzoyl-Ala-Arg
80°C, pH 6.5, 0.4 mM CoCl2
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667
N-carboxybenzoyl-Ala-Arg
80°C, pH 6.5, 0.4 mM CoCl2
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1391
substrate: N-carboxybenzoyl-Ala-Arg, 80°C, pH 6.5, 0.4 mM CoCl2
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5.3 - 7.3
pH 5.3: about 50% of maximal activity, pH 7.3: about 50% of maximal activity
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UniProt
brenda
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CBP1_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
499
0
59043
Swiss-Prot
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58000
2 * 58000, SDS-PAGE
59000
2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry
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homodimer
2 * 58000, SDS-PAGE
homodimer
2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry
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80
the overall structure of the holoenzyme is extremely thermostable. The activities of both the apo and holo enzyme exhibit a similar second-order decay over time, with 50% activity remaining after 40 min at 80°C
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purified in its inactive state by the addition of EDTA and dithiothreitol to purification buffers, and the activity is restored by the addition of Co2+
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Cheng, T.C.; Ramakrishnan, V.; Chan, S.I.
Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
Protein Sci.
8
2474-2486
1999
Pyrococcus furiosus (Q8U3L0), Pyrococcus furiosus
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History
3.4.17.B5 Pyrococcus furiosus carboxypeptidase
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