3.4.22.53: calpain-2
This is an abbreviated version!
For detailed information about calpain-2, go to the full flat file.
Word Map on EC 3.4.22.53
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3.4.22.53
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calpains
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calpastatin
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mu-calpain
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calcium-dependent
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ca2+-dependent
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proteinase
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myofibrillar
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cytoskeletal
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cataract
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zymography
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longissimus
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meat
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autolysis
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calpeptin
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tender
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casein
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cathepsins
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3.4.22.17
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postmortem
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calpain-mediated
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caspase-12
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lumborum
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autolyzed
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lens-specific
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talin
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alpha-spectrin
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canps
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cataractogenesis
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warner-bratzler
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spectrin
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slaughter
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semimembranosus
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calpain-specific
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desmin
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calpain-calpastatin
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lenses
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calpain-dependent
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atrogin-1
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medicine
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calpain-induced
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fodrin
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myofibril
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ca2+-activated
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calmodulin-like
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caseinolytic
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thoracis
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ca2+-requiring
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troponin-t
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micro-calpain
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calpain-like
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proteolyzed
- 3.4.22.53
- calpains
- calpastatin
- mu-calpain
-
calcium-dependent
-
ca2+-dependent
- proteinase
- myofibrillar
- cytoskeletal
- cataract
-
zymography
- longissimus
-
meat
-
autolysis
- calpeptin
-
tender
- casein
- cathepsins
-
3.4.22.17
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postmortem
-
calpain-mediated
- caspase-12
- lumborum
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autolyzed
-
lens-specific
- talin
- alpha-spectrin
-
canps
-
cataractogenesis
-
warner-bratzler
- spectrin
-
slaughter
- semimembranosus
-
calpain-specific
- desmin
-
calpain-calpastatin
- lenses
-
calpain-dependent
-
atrogin-1
- medicine
-
calpain-induced
- fodrin
- myofibril
-
ca2+-activated
-
calmodulin-like
-
caseinolytic
- thoracis
-
ca2+-requiring
-
troponin-t
- micro-calpain
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calpain-like
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proteolyzed
Reaction
broad endopeptidase specificity =
Synonyms
Cal II, calcium-activated neutral protease II, calpain 2, calpain II, calpain xCL-2 (Xenopus leavis), calpain-2, calpain-2-like, calpain2, CAPN II, CAPN2, CAPN2 g.p. (Homo sapiens), CPN2, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, human calpain 2, m-calpain, milli-calpain, mitochondrial m-calpain, nCL-2, rat calpain 2
ECTree
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Metals Ions
Metals Ions on EC 3.4.22.53 - calpain-2
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Al3+
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millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
Ba2+
Ca2+
Mg2+
Mn2+
Sr2+
Ba2+
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1 mM, decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+
Ca2+
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half maximal activity for retina and brain enzyme is 0.262 mM and 0.311 mM, maximal activity near 1 mM, no activity in presence of 0.03 mM
Ca2+
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treatment of the endoplasmic reticulum with Ca2+ (5 mM) dissociates m-calpain-calpastatin association leading to the activation of m-calpain
Ca2+
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best activator at 2.5 mM, maximal caseinolytic activity at 2.2 mM, half-maximal caseinolytic activity at 0.312 mM
Ca2+
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Kd-value: 0.325 mM. 25% of the difference in Kd values between mu-calpain and m-calpain can be ascribed to the N-terminal peptide of the large subunit, whereas the C-terminal EF-hand-containing domain IV accounts for 65% of the difference
Ca2+
Ca2+-binding must induce conformational changes that reorient the protease domains to form a functional active site
Ca2+
activates. The results support the hypothesis that Ca2+ induces movement of domains I and II closer together to form the functional active site of calpain
Ca2+
half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant
Ca2+
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Ca2+-induced calpain translocation to the membrane during ischemia is independent of its activation
Ca2+
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the Ca2+ dependency of mitochondrial m-calpain is similar to that of cytosolic m-calpain, 1 mM Ca2+ activates.
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1 mM decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+
Mn2+
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1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM
Mn2+
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5 mM 73.6% of the activation with 5 mM Ca2+. Synergistic activating effect with Ca2+
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2.5 mM, 66% of the activation obtained with Ca2+, maximal caseinolytic activity at 5.9 mM, half-maximal caseinolytic activity at 1.886 mM. Autolysis in presence of 5 mM Ca2+. The 80000 Da subunit is rapidly autolyzed in two smaller bands of 73000 Da and 69000 Da. The small subunit of 24000 da is degraded into three bands of 22000 Da, 19300 Da and 17800 Da. It is not clear whether autolysis is necessary for calpain to become proteolytically active
Sr2+
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1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM. Synergistic activating effect with Ca2+