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Information on EC 3.4.22.14 - actinidain
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3.4.22.14 actinidainSpecify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
actinidin, act d 1, actinidain, act1a-1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Act d 1
ACT1A-1
ACT1A-2
actinidia anionic protease
-
-
-
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actinidin
mercaptoproteinase A2
-
-
-
-
proteinase A2 of Actinidia chinensis
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-
-
-
actinidin
-
-
-
-
actinidin
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Similar to that of papain
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
39279-27-1
-
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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
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-
-
-
?
ethyl 2-pyridyl disulfide + H2O
?
-
reactivity probe, analysis of temperature-dependence of reaction kinetics
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-
?
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
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-
-
-
?
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
-
-
?
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
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-
?
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
?
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efficiently hydrolized at neutral or mild basic pH
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-
?
Fibrinogen + H2O
?
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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
?
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actinidin is ineffective on the heavy chain but has limited effects on the light chain
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-
?
atelocollagen + H2O
additional information
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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
?
-
-
the interplay of electrostatic and binding interactions determine the active center chemistry and catalytic activity
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-
?
additional information
?
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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
?
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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%
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-
?
additional information
?
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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%
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-
?
additional information
?
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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
-
-
?
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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-
?
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NATURAL SUBSTRATE
NATURAL 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
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
-
-
?
additional information
?
-
-
actinidain, from the juice of kiwi fruit, has no detrimental effect on either the motility of Trichuris muris or the nematode cuticle
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ba2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Ca2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Co2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
cystatin
-
hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit improved inhibition
-
Fe2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
human kininogen domain 2
-
hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit improved inhibition
-
KCl
-
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
-
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+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Mn2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
NaCl
-
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
-
potent, highly selective, irreversible
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide
-
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
-
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+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-cysteine
-
for activation of actinidin, 52 mM L-cysteine is added to the sample and the preparation incubated for 1 h at 45°C
L-cysteine
-
the enzyme is activated in 20 mM potassium phosphate buffer, pH 6.5 containing 52 mM L-cysteine and 2 mM EDTA (1:1 (v/v)) for 1 h at 45°C
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
The impact of Hayward green kiwifruit on dietary protein digestion and protein metabolism.
Acquired Immunodeficiency Syndrome
The nutritional and health attributes of kiwifruit: a review.
Anaphylaxis
Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to Kiwi with different clinical symptoms.
Food Hypersensitivity
A new approach for activation of the kiwifruit cysteine protease for usage in in-vitro testing.
Hypersensitivity
A new approach for activation of the kiwifruit cysteine protease for usage in in-vitro testing.
Hypersensitivity
Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells.
Hypersensitivity
Comparative modelling of major house dust mite allergen Der p I: structure validation using an extended environmental amino acid propensity table.
Hypersensitivity
Component-resolved diagnosis of kiwifruit allergy with purified natural and recombinant kiwifruit allergens.
Hypersensitivity
Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy.
Hypersensitivity
Diversity and relative levels of actinidin, kiwellin, and thaumatin-like allergens in 15 varieties of kiwifruit (Actinidia).
Hypersensitivity
Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy.
Hypersensitivity
IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries.
Hypersensitivity
Kiwifruit allergy: actinidin is not a major allergen in the United Kingdom.
Hypersensitivity
The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells.
Hypersensitivity, Immediate
Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0582
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C, Vmax: 2.14 miroM/sec
0.25
N-acetyl-L-Phe-Gly methyl ester
-
above 0.25 mM, at 4.3% acetonitrile, 25°C, pH 5.3, parameter for pre-steady-state acylation phase
0.543
N-acetyl-L-Phe-Gly methyl ester
-
25°C, pH 5.3, 8.3% acetonitrile parameter for pre-steady-state acylation phase
0.893
N-acetyl-L-Phe-Gly methyl ester
-
25°C, pH 5.3, 16.7% acetonitrile, parameter for pre-steady-state acylation phase
additional information
additional information
-
pH-dependence of Km-value
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
42.8
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C
additional information
additional information
-
pH-dependence of turnover number
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
730
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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