Literature summary for 3.4.22.52 extracted from

Doumit, M.E.; Koohmaraie, M.
Immunoblot analysis of calpastatin degradation: evidence for cleavage by calpain in postmortem muscle (1999), J. Anim. Sci., 77, 1467-1473.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Bos taurus	because the calcium concentration in postmortem muscle is high enough to activate mu-calpain, but not m-calpain, it seems reasonable to conclude that mu-calpain is responsible for postmortem degradation of calpastatin. Degradation of calpastatin by mu-calpain reduces calpain-inhibitory activity and is probably an important event in regulation of postmortem proteolysis, and, thus, meat tenderness	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	lamb	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
longissimus	postmortem muscle	Bos taurus	-
muscle	musculus longissimus, postmortem muscle	Bos taurus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	because the calcium concentration in postmortem muscle is high enough to activate mu-calpain, but not m-calpain, it seems reasonable to conclude that mu-calpain is responsible for postmortem degradation of calpastatin. Degradation of calpastatin by mu-calpain reduces calpain-inhibitory activity and is probably an important event in regulation of postmortem proteolysis, and, thus, meat tenderness	Bos taurus	?	-	?

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Release 2023.1 (January 2023)