3.4.22.14: actinidain
This is an abbreviated version!
For detailed information about actinidain, go to the full flat file.
Word Map on EC 3.4.22.14
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3.4.22.14
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papain
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kiwifruit
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proteinases
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allergen
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kiwi
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deliciosa
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catalytic-site
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hayward
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ficin
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bromelain
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thaumatin-like
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chymopapains
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hort16a
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brocklehurst
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cysteine-proteinase
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kiwellin
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medicine
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two-protonic-state
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active-centre
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synthesis
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food industry
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nutrition
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molecular biology
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biotechnology
- 3.4.22.14
- papain
- kiwifruit
- proteinases
- allergen
-
kiwi
- deliciosa
-
catalytic-site
- hayward
- ficin
- bromelain
-
thaumatin-like
- chymopapains
-
hort16a
-
brocklehurst
-
cysteine-proteinase
- kiwellin
- medicine
-
two-protonic-state
-
active-centre
- synthesis
- food industry
- nutrition
- molecular biology
- biotechnology
Reaction
Similar to that of papain =
Synonyms
Act d 1, ACT1A-1, ACT1A-2, Actd1, actinidain, actinidia anionic protease, actinidin, mercaptoproteinase A2, proteinase A2 of Actinidia chinensis
ECTree
3.4.22.14 actinidainAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.22.14 - actinidain
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Ba2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Ca2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Co2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
cystatin
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hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit improved inhibition
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Fe2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
human kininogen domain 2
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hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit improved inhibition
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KCl
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minimal activity at 0.5-0.8 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 0.8 M
LiCl
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minimal activity at 1.0-1.5 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.5 M
Mg2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Mn2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
NaCl
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minimal activity at 0.5-1.2 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.2 M
1-(L-trans-epoxysuccinylleucylamino)-4-guanidinobutane
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potent, highly selective, irreversible
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide
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conformational mobility of actinidin changes upon binding of the inhibitor E-64, leading to a sequence of events that enables water and ions to protrude into a newly formed cavity of the inhibited enzyme
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide
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in contrast to actinidin without inhibitor, the actinidinE-64 complex starts degrading 15 min after incubation in simulated gastric fluid (SGF) and is fully degraded after 60 min of incubation. In addition transition maximum temperature (Tm) of the actinidin-inhibitor complex is 61°C in contrast to Tm: 73.9° of actinidin without inhibitor
Zn2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
