3.4.17.B5: Pyrococcus furiosus carboxypeptidase

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For detailed information about Pyrococcus furiosus carboxypeptidase, go to the full flat file.

Reaction

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. =

Synonyms

PfuCP

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.17 Metallocarboxypeptidases

                3.4.17.B5 Pyrococcus furiosus carboxypeptidase

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Results	in table
1	AA Sequence
3	Inhibitors
1	kcat/KM [mM/s]
1	KM Value [mM]
1	Metals/Ions
3	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
1	Organism
1	pH Optimum
1	pH Range
1	Purification (Commentary)
1	Reaction
1	Reference
1	Specific Activity [micromol/min/mg]
19	Substrates and Products (Substrate)
2	Subunits
1	Synonyms
1	Temperature Optimum [°C]
1	Temperature Stability [°C]
1	Turnover Number [1/s]

Temperature Stability

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Temperature Stability on EC 3.4.17.B5 - Pyrococcus furiosus carboxypeptidase

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

80

Pyrococcus furiosus

Q8U3L0

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

721001