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Literature summary for 3.4.17.B1 extracted from

  • Occhipinti, E.; Martelli, P.L.; Spinozzi, F.; Corsi, F.; Formantici, C.; Molteni, L.; Amenitsch, H.; Mariani, P.; Tortora, P.; Casadio, R.
    3D structure of Sulfolobus solfataricus carboxypeptidase developed by molecular modeling is confirmed by site-directed mutagenesis and small angle X-ray scattering (2003), Biophys. J., 85, 1165-1175.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.17.B1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-metalloenzyme, contains about one Zn2+ per subunit Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
-
 Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Wild-type and mutated histidine-tagged enzyme are purified by Ni-chelate affinity chromatography Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-L-arginine + H2O
-
 Saccharolobus solfataricus benzoic acid + L-arginine
-
 ?

Subunits

Subunits Comment Organism
tetramer
-
 Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
CPSso
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Saccharolobus solfataricus