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Literature summary for 3.4.22.53 extracted from

  • Azuma, M.; Tamada, Y.; Kanaami, S.; Nakajima, E.; Nakamura, Y.; Fukiage, C.; Forsberg, N.E.; Duncan, M.K.; Shearer, T.R.
    Differential influence of proteolysis by calpain 2 and Lp82 on in vitro precipitation of mouse lens crystallins (2003), Biochem. Biophys. Res. Commun., 307, 558-563.
    View publication on PubMed
Search for more literature for 3.4.22.53

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutated calpain 2 C105A is driven in lens by coupling the mutated gene to the betaB1-crystallin promoter Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
calpastatin
-
 Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
crystallin + H2O Mus musculus alphaA crystallin in lenses from wild-type mice is proteolyzed by both calpain 2 and Lp82. Crystallins proteolyzed by calpain Lp82 are more susceptible to insolubilization than crystallins proteolyzed by calpain 2 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crystallin + H2O
-
 Mus musculus ?
-
 ?
crystallin + H2O alphaA crystallin in lenses from wild-type mice is proteolyzed by both calpain 2 and Lp82. Crystallins proteolyzed by calpain Lp82 are more susceptible to insolubilization than crystallins proteolyzed by calpain 2 Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
calpain 2
-
 Mus musculus