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Literature summary for 3.4.21.1 extracted from

  • Jelinek, B.; Katona, G.; Fodor, K.; Venekei, I.; Graf, L.
    The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin (2008), Protein J., 27, 79-87.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method with 0.1 M HEPES pH 7.0 as precipitant solution containing 30% PEG6000 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
SBTI-Sepharose column chromatography and HiPrep Sephacryl-100 column gel filtration Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-Ala-Ala-Pro-Lys-7-amido-4-methylcoumarin + H2O
-
Rattus norvegicus N-succinyl-Ala-Ala-Pro-Lys + 7-amino-4-methylcoumarin
-
?
N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O preferred substrate Rattus norvegicus N-succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
?

Synonyms

Synonyms Comment Organism
chymotrypsin-B
-
Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
using N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-metyhlcoumarin as a substrate Rattus norvegicus
9.5
-
using N-succinyl-Ala-Ala-Pro-Lys-7-amido-4-metyhlcoumarin as a substrate Rattus norvegicus