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Literature summary for 3.4.24.21 extracted from

  • Jing, Y.; Toubarro, D.; Hao, Y.; Simoes, N.
    Cloning, characterisation and heterologous expression of an astacin metalloprotease, Sc-AST, from the entomoparasitic nematode Steinernema carpocapsae (2010), Mol. Biochem. Parasitol., 174, 101-108.
    View publication on PubMed
Search for more literature for 3.4.24.21

Cloned(Commentary)

Cloned (Comment) Organism
recombinantly expressed in Escherichia coli Steinernema carpocapsae

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Steinernema carpocapsae
EGTA
-
 Steinernema carpocapsae
o-phenanthroline
-
 Steinernema carpocapsae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.86
-
 azocasein pH 7.5, 37°C, Vmax: 0.281 microM/min Steinernema carpocapsae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35200
-
 calculated from cDNA Steinernema carpocapsae

Organism

Organism UniProt Comment Textmining
Steinernema carpocapsae D2KBH9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azocasein + H2O
-
 Steinernema carpocapsae ?
-
 ?
Gelatin + H2O
-
 Steinernema carpocapsae ?
-
 ?

Synonyms

Synonyms Comment Organism
Sc-AST
-
 Steinernema carpocapsae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Steinernema carpocapsae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
27.9
-
 azocasein pH 7.5, 37°C Steinernema carpocapsae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Steinernema carpocapsae