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
-
allergen
-
kiwi
-
deliciosa
-
catalytic-site
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hayward
-
ficin
-
bromelain
-
thaumatin-like
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chymopapains
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hort16a
-
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
-
synthesis
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food industry
-
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
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results (Substrates Products
Substrates Products on EC 3.4.22.14 - actinidain
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(acetamido)ethylene 2'-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
2-(acetoxy)ethylene 2'-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
2-(N'-acetyl-D-phenylalanyl)hydroxyethylene 2'-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
2-(N'-acetyl-D-phenylalanylamino)ethylene 2'-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
2-(N'-acetyl-L-phenylalanyl)hydroxyethylene 2'-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
2-(N'-acetyl-L-phenylalanylamino)ethylene 2'-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
amylase + H2O
?
human salivary amylase is highly susceptible to digestion with actinidin. 83% of amylase function is lost within a 5 minutes incubation period at 37°C in mixtures of 1 part kiwifruit: 3 parts saliva
-
-
?
benzoyl-Gly p-nitrophenyl ester + H2O
benzoyl-Gly + p-nitrophenol
-
-
-
-
?
benzyloxycarbonyl 4-nitrophenyl ester + H2O
benzyl formate + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Gly p-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + p-nitrophenol
-
-
-
-
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
-
-
-
-
?
benzyloxycarbonyl-Lys p-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
-
?
ethyl 2-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
-
-
?
human occludin + H2O
?
human occludin is fragmented, and putative Act d1 cleavage sites are identified in extracellular loops of human occludin
-
-
?
Insulin B-chain + H2O
?
-
the enzyme cleaves most readily the carboxyl peptide bonds of those residues of the B-chain acylated by large hydrophobic residues - Val, Leu, or Phe, but not Tyr - and also the Arg22-Gly23 bond
-
-
?
kiwellin + H2O
KiTH + kissper
-
in vitro treatment of purified kiwellin, an allergenic protein formerly isolated from green kiwi fruit, with the protease actinidin from green kiwi fruit originates KiTH, a 20 kDa protein with 100% identity with the C-terminal region of kiwellin, and kissper, a described pore-forming peptide
-
-
?
N-acetyl-L-Phe-Gly methyl ester + H2O
?
-
stopped-flow spectral analysis of increasing content of co-solvent acetonitrile on kinetics
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitrophenol
Nalpha-benzoyl-L-Arg p-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
-
-
-
?
p-toluene-sulphonyl-L-glutamine p-nitrophenyl ester + H2O
p-toluene-sulphonyl-L-glutamine + 4-nitrophenol
-
-
-
-
?
Collagen + H2O
?
-
efficiently hydrolized at neutral or mild basic pH
-
-
?
Collagen + H2O
?
-
efficiently hydrolized at neutral or mild basic pH
-
-
?
Collagen type I + H2O
?
actinidin can hydrolyze collagen types I and II at neutral and alkaline pH
-
-
?
Collagen type I + H2O
?
the hydrolysis of types I and II collagen by actinidin under different pH conditions is monitored by SDS-PAGE: good digestion of type I collagen at pH 7 (phosphate buffer) or pH 8.5 (Tris-HCl buffer). In citrate buffer (pH 5.5), actinidin digests more than half of the collagen type I, but in acetate buffer (pH 4), the enzyme does not hydrolyze this substrate
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-
?
Collagen type I + H2O
?
-
actinidain cleaves between Gly1032 and Gly1033, limited hydrolysis by actinidain protease produces monomeric collagen, which consisted almost entirely of alpha1 and alpha2 chains
-
-
?
collagen type II + H2O
?
actinidin can hydrolyze collagen types I and II at neutral and alkaline pH
-
-
?
collagen type II + H2O
?
the hydrolysis of types I and II collagen by actinidin under different pH conditions is monitored by SDS-PAGE: good digestion of type I collagen at pH 7 (phosphate buffer) or pH 8.5 (Tris-HCl buffer). In citrate buffer (pH 5.5), or acetate buffer (pH 4), the enzyme does not hydrolyze this substrate
-
-
?
Fibrinogen + H2O
?
-
efficiently hydrolized at neutral or mild basic pH
-
-
?
Fibrinogen + H2O
?
-
efficiently hydrolized at neutral or mild basic pH
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitrophenol
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitrophenol
-
-
-
-
?
sheep IgG + H2O
?
-
actinidin is ineffective on the heavy chain but has limited effects on the light chain
-
-
?
sheep IgG + H2O
?
-
actinidin is ineffective on the heavy chain but has limited effects on the light chain
-
-
?
atelocollagen + H2O
additional information
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-
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actinaidin cleaves the atelocollagen molecule at specific sites on the inside of the interstrand cross-linking peptides. The actinidain-processed atelocollagen shows only monomeric alpha1 and alpha2 chains, with no beta and gamma chains, atelocollagen retains its typical triple helical structure
?
additional information
?
-
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the interplay of electrostatic and binding interactions determine the active center chemistry and catalytic activity
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-
?
additional information
?
-
-
actinidain, from the juice of kiwi fruit, has no detrimental effect on either the motility of Trichuris muris or the nematode cuticle
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-
?
additional information
?
-
-
actinidin compared with type II or IV collagenase isolated from intact human umbilical vein endothelial cells, hepatocytes, and thymic epithelial cells with viability more than 90%
-
-
?
additional information
?
-
actinidin compared with type II or IV collagenase isolated from intact human umbilical vein endothelial cells, hepatocytes, and thymic epithelial cells with viability more than 90%
-
-
?
additional information
?
-
-
digestibility of kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), is assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum: Act d 1 precipitates in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeds slowly. The residual precipitate redissolves completely in simulated duodenal fluid at pH 6.5 and is partially digested. Act d 1 and Act d 2 display nearly unchanged IgE binding abilities
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-
?
additional information
?
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the SDSPAGE profile of cream milk treated with actinidin reveals that both caseins, whey proteins and MFGF proteins are sharply digested by the enzyme
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-
?
