3.4.17.B1: Sulfolobus solfataricus carboxypeptidase

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For detailed information about Sulfolobus solfataricus carboxypeptidase, go to the full flat file.

Reaction

Release of basic, acidic and aromatic amino acids from the respective benzoylglycated and benzyloxycarbonylated amino acids. Slow hydrolysis of aliphatic amino acids. No activity with benzyloxycarbonyl-Pro and benzyloxycarbonyl-Trp =

Synonyms

carboxypeptidase, carboxypeptidase S1, CPS, cpsA, CPSso, M20.008, SSO1355, thermostable carboxypeptidase 1

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.17 Metallocarboxypeptidases

                3.4.17.B1 Sulfolobus solfataricus carboxypeptidase

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Results	in table
5	Activating Compound
1	AA Sequence
3	Application
3	Cloned(Commentary)
1	Crystallization (Commentary)
7	General Stability
6	Inhibitors
25	KM Value [mM]
2	Localization
8	Metals/Ions
4	Molecular Weight [Da]
12	Natural Substrates/ Products (Substrates)
12	Organic Solvent Stability
62	Organism
5	pH Optimum
1	pH Range
1	pH Stability
1	pI Value
5	Protein Variants
8	Purification (Commentary)
1	Reaction
5	Reaction Type
15	Reference
11	Specific Activity [micromol/min/mg]
1	Storage Stability
62	Substrates and Products (Substrate)
4	Subunits
18	Synonyms
7	Temperature Optimum [°C]
2	Temperature Range [°C]
17	Temperature Stability [°C]
24	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.17.B1 - Sulfolobus solfataricus carboxypeptidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

3D structure is developed by a molecular modeling approach. The Monte Carlo method is used to compare the crystallographic coordinates of the possible molecular structures for the enzyme with the small angle X-ray scattering profiles

Saccharolobus solfataricus

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