3.4.22.54: calpain-3
This is an abbreviated version!
For detailed information about calpain-3, go to the full flat file.
Word Map on EC 3.4.22.54
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3.4.22.54
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calpains
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dystrophy
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muscular
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limb-girdle
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girdle
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lgmd2a
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limb
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calpainopathy
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titin
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calpastatin
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myopathy
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dysferlin
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tender
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autolytic
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sarcomere
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mu-calpains
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sarcoglycans
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myofibrillar
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telethonin
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scapular
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alpha-sarcoglycan
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merosin
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autolyzed
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caveolin-3
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nebulin
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lumborum
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m-lines
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dysferlinopathy
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sarcoglycanopathy
- 3.4.22.54
- calpains
- dystrophy
- muscular
-
limb-girdle
-
girdle
-
lgmd2a
- limb
-
calpainopathy
- titin
- calpastatin
- myopathy
-
dysferlin
-
tender
-
autolytic
- sarcomere
- mu-calpains
-
sarcoglycans
- myofibrillar
-
telethonin
-
scapular
-
alpha-sarcoglycan
-
merosin
-
autolyzed
-
caveolin-3
-
nebulin
- lumborum
-
m-lines
-
dysferlinopathy
- sarcoglycanopathy
Reaction
broad endopeptidase activity =
Synonyms
C3DIV, calcium-activated neutral proteinase 3, Calp3, calpain 3, calpain 3 (p94), calpain 3 domain IV, calpain 3/p94, calpain L3, calpain M, calpain p94, calpain-3, calpain3, CANP 3, CAPN3, Cn94, MP78, Mp84, muscle calpain, muscle-specific calcium-activated neutral protease 3, muscle-specific calpain, nCL-1, p94, p94-calpain, p94/calpain 3, skeletal muscle-specific calpain
ECTree
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Metals Ions
Metals Ions on EC 3.4.22.54 - calpain-3
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Ca2+
Na+
Ca2+
regulated by Ca2+, contains 2 EF-hand calcium-binding domains. Activated by micromolar concentrations of calcium
Ca2+
regulated by Ca2+, contains 2 EF-hand calcium-binding domains. Activated by micromolar concentrations of calcium
Ca2+
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P94 insertion sequence 1 is a propeptide that must be autoproteolytically cleaved to provide access of substrates and inhibitors to the enzyme's active site. Initial autoproteolytic cleavage is an intramolecular reaction, transient binding of two Ca2+ ions to the core would be sufficient to promote the reaction that is facilitated by having the scissile peptide close to the active site cysteine. The second autolytic cleavage is much slower and requires higher Ca2+ levels, consistent with it being an intermolecular reaction. High increase in hydrolysis rate when Ca2+ is increased from 10 to 100 mM
Ca2+
regulated by Ca2+, contains 2 EF-hand calcium-binding domains. Activated by micromolar concentrations of calcium
Ca2+
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autolysis of skeletal muscle-specific calpain does not require Ca2+, calpastatinolysis occurs in a Ca2+-dependent manner
Ca2+
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at less than 50 nM Ca2+ calpain-3 remains nonactivated, at 200 nM Ca2+ calpain-3 becomes active
Ca2+
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calpain 3/p94 is activated by Ca2+ and undergoes very rapid autolytic degradation even in the absence of Ca2+
Ca2+
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calpain-3 autolyzes (becoming proteolytically active) in a tightly calcium-dependent manner. It remains in its nonactivated full-length form if [Ca2+] is maintained at up to 50 nM, the normal resting level, even with brief increases to 0.002-0.02 mM during repeated tetanic contractions, but it becomes active (though still bound) if [Ca2+] is kept slightly elevated at 200 nM (about 20% autolysis in 1 h). Calpain-3 does not spontaneously autolyze even when free in solution with 200 nM Ca2+ for up to 60 min
Ca2+
regulated by Ca2+, contains 2 EF-hand calcium-binding domains. Activated by micromolar concentrations of calcium
Na+
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calpain 3/p94 is activated by Na+ and undergoes Na+-dependent, but not Cs+-dependent, autolysis in the absence of Ca2+. Na+ and Ca2+ complementarily activate autolysis of calpain3/p94 at physiological concentrations. Na+ and Ca2+ direct calpain3/p94 to proteolyze different substrates