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Literature summary extracted from

  • Krauhs, E.; Dörsam, H.; Little, M.; Zwilling, R.; Ponstingl, H.
    A protease from Astacus fluviatilis as an aid in protein sequencing (1982), Anal. Biochem., 119, 153-157.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.24.21 Very resistant to self-degradation even upon prolonged incubation for several days Astacus astacus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.21 soluble
-
 Astacus astacus
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.21 Astacus astacus
-
 i.e. Astacus fluviatilis
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.21 two closely related forms of slightly different electrophoretic mobility Astacus astacus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.21 cardia
-
 Astacus astacus
-
3.4.24.21 digestive juice
-
 Astacus astacus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.21 denatured chains of alpha-tubulin + H2O cleavage sites, overview Astacus astacus hydrolyzed alpha-tubulin chains
-
 ?
3.4.24.21 denatured chains of beta-tubulin + H2O cleavage sites, overview Astacus astacus hydrolyzed beta-tubulin chains
-
 ?
3.4.24.21 additional information hydrolyzes peptide bonds on the amino side of the small uncharged residues Ala, Thr, Ser, Gly and Val Astacus astacus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.21 20
-
 assay at Astacus astacus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.21 additional information
-
 pI: 4 Astacus astacus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.24.21 4
-
 below, rapid and irreversible inactivation Astacus astacus