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
-
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
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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
3.4.22.53 calpain-2Advanced search results
results (
results (Engineering
Engineering on EC 3.4.22.53 - calpain-2
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C105S
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mutant enzyme of mutant large subunit m-C105S-80K, coexpressed with 30000 Da subunit in Sf-9 cells does not degrade casein nor the artificial substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide. The mutant enzyme does not show autolytic activity with Ca2+
K390R
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overexpression of K390R mutant fails to increase the calpain activity since sumoylation at K390 is important for calpain-2 activity
C105S
D346E
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
D362K
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
E504S
G423R
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
K225S
mutation decreases specific activity to 88% compared to wild-type enzyme
K226S
Ca2+ concentration required for half-maximal activity is 0.226 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230E
K230S
K234E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K234S
K234W
Ca2+ concentration required for half-maximal activity is 0.159 mM compared to 0.242 mM for the wild-type enzyme
R417W
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
S50D
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mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S50E
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mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S67E
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mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
T344M
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
T70E
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mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
additional information
C105S
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inactive mutant enzyme. The mutant enzyme provides a purified calpain, that is stable to autolysis and oxidation, which is likely to facilitate crystallization in both the presence and absence of calcium
E504S
Ca2+ concentration required for half-maximal activity is 0.129 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
E504S
mutation decreases specific activity to 90% compared to wild-type enzyme
K230E
Ca2+ concentration required for half-maximal activity is 0.256 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K230S
Ca2+ concentration required for half-maximal activity is 0.261 mM compared to 0.242 mM for the wild-type enzyme
K234S
Ca2+ concentration required for half-maximal activity is 0.183 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K234S
mutation decreases specific activity to 81% compared to wild-type enzyme
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
additional information
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replacement of the five m-calpain residues 517-521, Glu-Ala-Asn-Ile-Glu by the corresponding six mu-calpain residues 528-533, Gln-Ala-Asn-Leu-Pro-Asp, replacement of three m-calpain residues 639-641, Pro-Cys-Gln, by the corresponding three mu-calpain residues 651-653, Asn-Lys-Lys, or replacement of two m-calpain residues 578-579, Lys-Ile by the corresponding mu-calpain residues 590-591, Arg-Ser. Mutations do not affect the expression and Kd values of the resultant calpains. In a series of hybrid mu/m large-subunit calpains, the Kd values decrease progressively towards that of mu-calpain as the portion of mu-type sequence increases from 0 to 90%
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
