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Literature summary for 3.4.17.B5 extracted from

  • Cheng, T.C.; Ramakrishnan, V.; Chan, S.I.
    Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus (1999), Protein Sci., 8, 2474-2486.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.17.B5

Inhibitors

Inhibitors Comment Organism Structure
DTT 2 mM, complete inhibition Pyrococcus furiosus
EDTA 1 mM, complete inhibition. Inhibition is fully reversible upon 50fold dilution and re-activation by Co2+ Pyrococcus furiosus
additional information the serine protease inhibitor phenylmethylsulfonyl fluoride has no effect on the activity Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.9
-
 N-carboxybenzoyl-Ala-Arg 80°C, pH 6.5, 0.4 mM CoCl2 Pyrococcus furiosus

Metals/Ions

Metals/Ions Comment Organism Structure
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+ Pyrococcus furiosus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
 2 * 58000, SDS-PAGE Pyrococcus furiosus
59000
-
 2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry Pyrococcus furiosus
128000
-
 gel filtration Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pyrococcus furiosus the enzyme is involved in digestion and protein turnover ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U3L0
-
-

Purification (Commentary)

Purification (Comment) Organism
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+ Pyrococcus furiosus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1391
-
 substrate: N-carboxybenzoyl-Ala-Arg, 80°C, pH 6.5, 0.4 mM CoCl2 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
-
 Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro + L-phenylalanine
-
 ?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + H2O
-
 Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + L-histidine
-
 ?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
-
 Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + L-leucine
-
 ?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + H2O
-
 Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + L-leucine
-
 ?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + H2O
-
 Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + L-valine
-
 ?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O
-
 Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + L-tyrosine
-
 ?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O stepwise hydrolysis of up to seven residues from the C-terminus Pyrococcus furiosus Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + L-serine
-
 ?
additional information the enzyme is involved in digestion and protein turnover Pyrococcus furiosus ?
-
 ?
additional information no activity with N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Glu Pyrococcus furiosus ?
-
 ?
N-carboxybenzoyl-Ala-Ala + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-alanine
-
 ?
N-carboxybenzoyl-Ala-Arg + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-arginine
-
 ?
N-carboxybenzoyl-Ala-Ile + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-isoleucine
-
 ?
N-carboxybenzoyl-Ala-Leu + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-leucine
-
 ?
N-carboxybenzoyl-Ala-Lys + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-lysine
-
 ?
N-carboxybenzoyl-Ala-Met + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-methionine
-
 ?
N-carboxybenzoyl-Ala-Phe + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-phenylalanine
-
 ?
N-carboxybenzoyl-Ala-Trp + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-tryptophan
-
 ?
N-carboxybenzoyl-Ala-Tyr + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-tyrosine
-
 ?
N-carboxybenzoyl-Ala-Val + H2O
-
 Pyrococcus furiosus N-carboxybenzoyl-Ala + L-valine
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 58000, SDS-PAGE Pyrococcus furiosus
homodimer 2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry Pyrococcus furiosus

Synonyms

Synonyms Comment Organism
PfuCP
-
 Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
-
 Pyrococcus furiosus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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 Pyrococcus furiosus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
600
-
 N-carboxybenzoyl-Ala-Arg 80°C, pH 6.5, 0.4 mM CoCl2 Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2 6.6
-
 Pyrococcus furiosus

pH Range

pH Minimum pH Maximum Comment Organism
5.3 7.3 pH 5.3: about 50% of maximal activity, pH 7.3: about 50% of maximal activity Pyrococcus furiosus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
667
-
 N-carboxybenzoyl-Ala-Arg 80°C, pH 6.5, 0.4 mM CoCl2 Pyrococcus furiosus