Information on EC 4.4.1.4 - alliin lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.4.1.4
-
RECOMMENDED NAME
GeneOntology No.
alliin lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
-
-
elimination
-
-
of RSH, C-S bond cleavage
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(Z)-butanethial-S-oxide biosynthesis
-
-
(Z)-phenylmethanethial S-oxide biosynthesis
-
-
alliin metabolism
-
-
ethiin metabolism
-
-
methiin metabolism
-
-
propanethial S-oxide biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
S-alkyl-L-cysteine S-oxide alkyl-sulfenate-lyase (2-aminoacrylate-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-77-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Allium cepa * Allium altyncolicum
-
-
-
Manually annotated by BRENDA team
Allium cepa * Allium chevsuricum
-
-
-
Manually annotated by BRENDA team
Allium cepa * Allium globosum
-
-
-
Manually annotated by BRENDA team
Allium cepa * Allium oliquum
-
-
-
Manually annotated by BRENDA team
Allium cepa * Allium saxatile
-
-
-
Manually annotated by BRENDA team
Allium cepa * Allium senescens
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Trautv.
-
-
Manually annotated by BRENDA team
Trautv.
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from a soil sample
-
-
Manually annotated by BRENDA team
Ensifer adhaerens FERM P-19486
isolated from a soil sample
-
-
Manually annotated by BRENDA team
Leucocoryne odorata
-
-
-
Manually annotated by BRENDA team
Penicillium corymbiferum
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
lachrymatory factor synthase and alliinase function in tandem, with the alliinase furnishing the sulfenic acid substrate on which the lachrymatory factor synthase acts. The lachrymatory factor synthase modulates the formation of biologically active thiosulfinates that are downstream of the alliinase in a manner dependent upon the relative concentrations of the lachrymatory factor synthase and the alliinase. These observations suggest that manipulation of lachrymatory factor synthase-to-alliinase ratios in plants displaying this system may provide a means by which to rationally modify organosulfur small molecule profiles to obtain desired flavor and/or odor signatures, or increase the presence of desirable biologically active small molecules
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-(S)-allyl-L-cysteine sulfoxide
2-propenyl 2-propenethiosulfinate + pyruvate + NH3
show the reaction diagram
-
-
i.e. allicin
-
?
(+)-alliin
allicin + pyruvic acid + NH3
show the reaction diagram
(+)-S-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
(+)-S-propyl-L-cysteine sulfoxide
propane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
(+/-)-(1-methyl)-L-cysteine sulfoxide
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
(+/-)-alliin
allicin + pyruvic acid + NH3
show the reaction diagram
(+/-)-S-methyl-L-cysteine sulfoxide
?
show the reaction diagram
-
high activity
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
(-)-alliin
allicin + pyruvic acid + NH3
show the reaction diagram
(-)cystathionine
?
show the reaction diagram
-
3% of the activity with desglutamyl-lentinic acid
-
-
?
(2R)-2-amino-3-(1-phenylethylsulfinyl)propanoic acid
(1-phenylethyl)sulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(2R)-2-amino-3-(2-methylbenzylsulfinyl)propanoic acid
(2-methylbenzyl)sulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(2R)-2-amino-3-(4-chlorobenzylsulfinyl)propanoic acid
(4-chlorobenzyl)sulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(2R)-2-amino-3-(4-methylbenzylsulfinyl)propanoic acid
(4-methylbenzyl)sulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(2R)-2-amino-3-(phenethylsulfinyl)propanoic acid
phenethylsulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(2R)-2-amino-3-(phenylsulfinyl)propanoic acid
phenylsulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
(R)-S-(2-pyridyl)cysteine N-oxide
2-sulfanylpyridine N-oxide + 2-aminoacrylate
show the reaction diagram
-
-
2-sulfanylpyridine N-oxide can spontaneously rearrange into tautomeric and more stable N-hydroxypyridine-(1H)-thione, which can be transformed to 2-(methyldithio)pyridine N-oxide, 2-[(methylthio)methyldithio]pyridine N-oxide, di(2-pyridyl) disulfide N-oxide, and di(2-pyridyl) disulfide N,N'-dioxide
-
?
(S)-(2-pyrrolyl)cysteine
2-pyrrolesulfenic acid + 2-aminoacrylate
show the reaction diagram
(S)-(2-pyrrolyl)cysteine S-oxide
2-pyrrolesulfenic acid + 2-aminoacrylate
show the reaction diagram
(S)-(3-pyrrolyl)cysteine S-oxide
3-pyrrolesulfenic acid + 2-aminoacrylate
show the reaction diagram
2 alliin + H2O
allicin + 2 pyruvate + 2 NH3
show the reaction diagram
2-hydroxyethiin
(2-hydroxyethyl)sulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
4-mercaptopyridine
?
show the reaction diagram
-
-
-
-
?
alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
alliin
allicin + ?
show the reaction diagram
-
-
pure allicin has significantly stronger in vitro inhibitory effect on the growth of six tested fungi (Candida albicans, Cryputococcus neoformans, Trichophyton rubum, Microsporum gypseum, Microsporum canis and Epidermophyton floccosum) than alliin and alliinase
-
?
alliin + H2O
allicin + pyruvate + NH4+
show the reaction diagram
beta-chloro-L-Ala
?
show the reaction diagram
-
95% of the activity with desglutamyl-lentinic acid
-
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
cystine
?
show the reaction diagram
-
-
-
-
?
desglutamyl-lentinic acid
?
show the reaction diagram
-
-
-
-
?
djenkolic acid
?
show the reaction diagram
-
-
-
-
?
ethiin
ethanesulfenic acid + pyruvate + NH3
show the reaction diagram
isoalliin
? + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
L-(+)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
L-(+)-isoalliin
?
show the reaction diagram
L-(+)-S-(2-pyridyl)-cysteine sulfoxide + H2O
?
show the reaction diagram
-
the amount of this cysteine sulfoxide, related to the fresh weight of bulbs, is between 0.13 and 0.44%
-
-
?
L-(-)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
L-Cys
?
show the reaction diagram
-
0.4% of the activity with desglutamyl-lentinic acid
-
-
?
L-Cys sulfinic acid
?
show the reaction diagram
-
0.5% of the activity with desglutamyl-lentinic acid
-
-
?
L-cysteine
?
show the reaction diagram
L-cystine
?
show the reaction diagram
L-cystine
pyruvate + NH4+ + S2- + cysteine
show the reaction diagram
-
cystine lyase activity of the enzyme alliinase
-
-
?
methiin
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
methiin
methanesulfenic acid + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
methiin + H2O
?
show the reaction diagram
-
-
-
-
?
petiveriin
benzylsulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form petivericin. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
propiin
propane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
propiin
propylsulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
S-(+)-allyl-L-cysteine sulfoxide + H2O
allyl 2-propenethiosulphinate
show the reaction diagram
-
-
-
-
?
S-(1-butenyl)-L-cysteine sulfoxide
?
show the reaction diagram
S-(2-chloro-4-nitrophenyl)-L-Cys
?
show the reaction diagram
-
-
-
-
?
S-(2-chloro-6-nitrophenyl)-L-Cys
?
show the reaction diagram
-
-
-
-
?
S-(2-hydroxyethyl)-L-cysteine sulfoxide
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-(methylthiomethyl)cysteine 4-oxide
(methylthio)methane-sulfenic acid + 2-aminoacrylate
show the reaction diagram
-
i.e. marasmin
-
-
?
S-allyl-Cys sulfoxide
allicin + ?
show the reaction diagram
-
-
-
-
?
S-allyl-L-Cys
?
show the reaction diagram
-
4% of the activity with desglutamyl-lentinic acid
-
-
?
S-allyl-L-Cys sulfoxide
2-propene-thioic acid + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-allyl-L-Cys sulfoxide
allicin + ?
show the reaction diagram
-
-
-
-
?
S-allyl-L-Cys sulfoxide
ethylenesulfenic acid + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-allyl-L-cysteine
?
show the reaction diagram
-
high activity
-
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
S-benzyl-L-cysteine sulfoxide
phenylmethanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-butyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
?
S-ethyl-cysteine sulfoxide
diethyldisulfide-S-monoxide + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys
?
show the reaction diagram
S-ethyl-L-Cys sulfoxide
ethanesulfenic acid + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
S-ethyl-L-Cys sulfoxide
ethylsulfenic acid + pyruvate + NH3
show the reaction diagram
S-ethyl-L-cysteine
?
show the reaction diagram
S-methyl-cysteine sulfoxide
dimethyldisulfide-S-monoxide + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-methyl-L-Cys
?
show the reaction diagram
-
0.9% of the activity with desglutamyl-lentinic acid
-
-
?
S-methyl-L-Cys sulfone
?
show the reaction diagram
-
6% of the activity with desglutamyl-lentinic acid
-
-
?
S-methyl-L-Cys sulfoxide
?
show the reaction diagram
S-methyl-L-Cys sulfoxide
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine
?
show the reaction diagram
S-methyl-L-cysteine sulfoxide
pyruvate + ?
show the reaction diagram
-
-
-
?
S-phenyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
?
S-propenyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
?
S-propyl-cysteine sulfoxide
dipropyldisulfide-S-monoxide + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-propyl-L-Cys
?
show the reaction diagram
S-propyl-L-Cys sulfoxide
?
show the reaction diagram
S-propyl-L-Cys sulfoxide
propanesulfenic acid + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
trans-(+)-S-(1-propenyl)-L-cysteine sulfoxide
?
show the reaction diagram
trans-(+)-S-propenyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(+)-(S)-allyl-L-cysteine sulfoxide
2-propenyl 2-propenethiosulfinate + pyruvate + NH3
show the reaction diagram
-
-
i.e. allicin
-
?
(+/-)-alliin
allicin + pyruvic acid + NH3
show the reaction diagram
-
-
-
-
?
(-)-alliin
allicin + pyruvic acid + NH3
show the reaction diagram
-
i.e. (-)-S-allyl-L-cysteine sulfoxide, the enzyme is more selectively for (-)-alliin than for (+)-alliin, the enzyme can selectively decompose (-)-alliin, whereas the level of (+)-alliin remains unchanged at least during 30-min incubation
-
-
?
(R)-S-(2-pyridyl)cysteine N-oxide
2-sulfanylpyridine N-oxide + 2-aminoacrylate
show the reaction diagram
-
-
2-sulfanylpyridine N-oxide can spontaneously rearrange into tautomeric and more stable N-hydroxypyridine-(1H)-thione, which can be transformed to 2-(methyldithio)pyridine N-oxide, 2-[(methylthio)methyldithio]pyridine N-oxide, di(2-pyridyl) disulfide N-oxide, and di(2-pyridyl) disulfide N,N'-dioxide
-
?
(S)-(2-pyrrolyl)cysteine
2-pyrrolesulfenic acid + 2-aminoacrylate
show the reaction diagram
2 alliin + H2O
allicin + 2 pyruvate + 2 NH3
show the reaction diagram
-
-
-
-
?
2-hydroxyethiin
(2-hydroxyethyl)sulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
L-(+)-S-(2-pyridyl)-cysteine sulfoxide + H2O
?
show the reaction diagram
-
the amount of this cysteine sulfoxide, related to the fresh weight of bulbs, is between 0.13 and 0.44%
-
-
?
methiin
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
methiin + H2O
?
show the reaction diagram
-
-
-
-
?
petiveriin
benzylsulfanol + pyruvate + NH4+
show the reaction diagram
-
-
The sulfenic acid condenses with loss of water to form petivericin. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
S-(1-butenyl)-L-cysteine sulfoxide
?
show the reaction diagram
S-(2-hydroxyethyl)-L-cysteine sulfoxide
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-(methylthiomethyl)cysteine 4-oxide
(methylthio)methane-sulfenic acid + 2-aminoacrylate
show the reaction diagram
-
i.e. marasmin
-
-
?
S-allyl-Cys sulfoxide
allicin + ?
show the reaction diagram
-
-
-
-
?
S-allyl-L-Cys sulfoxide
2-propene-thioic acid + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
-
-
-
-
-
S-benzyl-L-cysteine sulfoxide
phenylmethanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
trans-(+)-S-propenyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Aminooxyacetate
-
-
Dicyclohexylcarbodiimide
-
-
DL-homocysteine
-
competitive
hydrazine
-
-
hydroxylamine
Iodine
-
-
iodoacetate
-
-
L-Cys
-
competitive
L-cysteine ethyl ester
-
competitive
N-acetyl-L-Cys
-
competitive
N-Acetylimidazole
-
slightly decreases activity
N-bromosuccinimide
-
rapidly and completely inactivates
Penicillamine
-
competitive inhibitor
Phenylmercury acetate
-
-
rotenone
-
-
S-alkyl derivatives of L-Cys
-
competitive
S-allyl-L-Cys
-
competitive
S-ethyl-L-Cys
-
competitive
S-propyl-L-Cys
-
competitive
S-tert-butyl-L-Cys
-
competitive
Succinic anhydride
-
slightly decreases activity
Trinitrobenzenesulfonic acid
-
2.5 mM, 50% inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
low-frequency and low-intensity ultrasound accelerates alliinase-catalysed synthesis of allicin by about 42.8% in freshly crushed garlic cloves, without affecting the enzyme's temperature optimum
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.7
(+)-alliin
-
pH 7.0, 30C
-
0.42 - 1.79
(+)-S-(2-propenyl)-L-cysteine sulfoxide
1.493 - 2.3
(+/-)-alliin
1
(-)-alliin
-
about, below, pH 7.0, 30C
28.6
(2R)-2-amino-3-(1-phenylethylsulfinyl)propanoic acid
-
pH 8.0, 22C
9.29
(2R)-2-amino-3-(2-methylbenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
2.11
(2R)-2-amino-3-(4-chlorobenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
0.72
(2R)-2-amino-3-(4-methylbenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
0.33
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid
-
pH 8.0, 22C
0.23
(2R)-2-amino-3-(phenethylsulfinyl)propanoic acid
-
pH 8.0, 22C
1.96
(2R)-2-amino-3-(phenylsulfinyl)propanoic acid
-
pH 8.0, 22C
0.5
2-hydroxyethiin
-
pH 8.0, 22C
1.32 - 1.418
4-mercaptopyridine
2.9 - 4.22
alliin
2.2 - 9.7
cystine
0.06
desglutamyl-lentinic acid
-
-
0.88 - 3.08
L-(+)-alliin
2.8
L-(-)-alliin
-
enzyme from garlic powder
1.94 - 2.65
L-cystine
13.9
methiin
-
pH 8.0, 22C
0.39
petiveriin
-
pH 8.0, 22C
0.25
propiin
-
pH 8.0, 22C
0.4 - 0.5
S-(2-chloro-4-nitrophenyl)-L-Cys
0.7
S-(2-chloro-6-nitrophenyl)-L-Cys
-
alliin lyase I
1.1 - 24.1
S-allyl-L-Cys sulfoxide
2.5 - 68.4
S-ethyl-L-Cys sulfoxide
47 - 96.6
S-methyl-L-Cys sulfoxide
7.6 - 9.9
S-phenyl-L-Cys sulfoxide
2.6 - 3
S-propenyl-L-Cys sulfoxide
0.6 - 22
S-propyl-L-Cys sulfoxide
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008 - 0.015
(+/-)-alliin
8.18
(2R)-2-amino-3-(1-phenylethylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
14.33
(2R)-2-amino-3-(2-methylbenzylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
10.65
(2R)-2-amino-3-(4-chlorobenzylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
2.67
(2R)-2-amino-3-(4-methylbenzylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
2.48
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
1.75
(2R)-2-amino-3-(phenethylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
6.48
(2R)-2-amino-3-(phenylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
4.2
2-hydroxyethiin
Petiveria alliacea
-
pH 8.0, 22C
0.00185 - 0.0028
4-mercaptopyridine
20.67
alliin
Petiveria alliacea
-
pH 8.0, 22C
15.1
methiin
Petiveria alliacea
-
pH 8.0, 22C
4.47
petiveriin
Petiveria alliacea
-
pH 8.0, 22C
1.96
propiin
Petiveria alliacea
-
pH 8.0, 22C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.331 - 0.595
(+/-)-alliin
2.49
(2R)-2-amino-3-(1-phenylethylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
38558
13.4
(2R)-2-amino-3-(2-methylbenzylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
38559
44
(2R)-2-amino-3-(4-chlorobenzylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
38364
32.3
(2R)-2-amino-3-(4-methylbenzylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
38363
65.7
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
26988
66.5
(2R)-2-amino-3-(phenethylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
39641
28.9
(2R)-2-amino-3-(phenylsulfinyl)propanoic acid
Petiveria alliacea
-
pH 8.0, 22C
39640
73.4
2-hydroxyethiin
Petiveria alliacea
-
pH 8.0, 22C
27240
0.084 - 0.11
4-mercaptopyridine
42.8
alliin
Petiveria alliacea
-
pH 8.0, 22C
8582
1.09
methiin
Petiveria alliacea
-
pH 8.0, 22C
13704
100
petiveriin
Petiveria alliacea
-
pH 8.0, 22C
40128
68.8
propiin
Petiveria alliacea
-
pH 8.0, 22C
23224
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
Trinitrobenzenesulfonic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.17
Penicillium corymbiferum
-
-
23.2
-
-
59 - 1003
-
purified catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibodies, pH 7.0, 35C, substrate (+/-)-alliin
90
-
purified enzyme, pH 7.0, 30C, after gel filtration step
102.5
-
purified enzyme, pH 7.0, 30C, after second anion exchange chromatography step
119.7
-
-
129.9
-
enzyme from garlic powder
2989
-
purifed native enzyme, pH 7.0, 35C, substrate (+/-)-alliin
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
free alliinase, 25C
6.5 - 7
-
sodium phosphate buffer
6.5
Penicillium corymbiferum
-
-
7 - 8
-
enzyme from garlic powder
7.4 - 8.5
-
-
7.4
-
potassium phosphate buffer
8 - 8.5
-
Tris/HCl buffer
8.1
-
Tris-HCl buffer
8.6
-
sodium diphosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
-
immobilized alliinase
5 - 8
Allium cepa * Allium oliquum
-
about 50% of maximal activity at pH 6.5 and 8.0
5 - 10
-
active in the range
5.5 - 8
-
about 50% of maximal activity at pH 6.0 and 8.0
5.5 - 7.5
Allium cepa * Allium chevsuricum
-
about 50% of maximal activity at pH 5.5 and 7.5
5.5 - 8
Allium cepa * Allium globosum
-
about 50% of maximal activity at pH 6.5 and 8.0
5.5 - 7.5
Allium cepa * Allium saxatile
-
about 50% of maximal activity at pH 6.5 and 8.0
5.5 - 8
Allium cepa * Allium senescens
-
about 50% of maximal activity at pH 6.5 and pH 8.0
5.5 - 8.5
5.5 - 8
-
half-maximal activity at pH 5.5 and at pH 8.0
5.5 - 8.5
5.5 - 10.5
-
activity range, profile overview
5.5 - 8
Penicillium corymbiferum
-
about 20% of maximal activity at pH 5.5 and pH 8.0
6 - 8.5
-
half-maximal activity at pH 6.0 and at pH 8.5
6.5 - 8
Allium cepa * Allium altyncolicum
-
about 50% of maximal activity at pH 6.5 and 8.0
6.5 - 8.5
7 - 11
-
pH 7.0: about 30% of maximal activity, pH 11.0: about 60% of maximal activity
additional information
-
the enzyme activity is immediately and irreversibly destroyed below pH 3.5, the usual pH of gastric juice
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
-
-
30
-
free alliinase
34
Allium cepa * Allium altyncolicum
-
-
37
-
assay at
52
-
with the most preferred substrate petiveriin, Petiveria alliacea alliinase shows 80% higher activity at 37C and 100% higher activity at 52C than at ambient temperature (25C). Even at 67C, alliinase activity is still 19% higher than that observed at room temperature, indicating that the alliinase retains significant functionality over a broad range of temperature and possesses a high overall intrinsic thermal stability
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 60
-
no activity at 0C, highly reduced activity at 60C, maximal activity at 30C
20 - 50
additional information
-
the enzyme activity declines rapidly at body temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 4.7
-
alliinase I, isoelectric focusing
4.78
-
chromatofocusing
6.9
-
alliinase II, isoelectric focusing
9.47
-
calculated
additional information
-
between 6.0 and 7.0
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
alliinase and lectin are the predominant proteins in nectar
Manually annotated by BRENDA team
Penicillium corymbiferum
-
-
Manually annotated by BRENDA team
-
the enzyme predominantly accumulates in the bundle sheath cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
the enzyme alliinase resides in microcompartments separated by thin membranes, and is thus physically kept apart from its substrate alliin
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
-
alliinase I, gel filtration
57500
-
alliinase II, gel filtration
67000
-
gel filtration
85000
-
gel filtration
90000
-
-
96000
-
gel filtration
103000
-
-
105000 - 111000
-
non-denaturing PAGE
106000 - 110000
-
enzyme from garlic powder, non-denaturing PAGE
136900
-
calculation from amino acid composition and carbohydrate content
145100
-
gel-filtration chromatography
150000
-
sedimentation equilibrium centrifugation
200000
-
gel filtration
218700
-
SDS-PAGE, this is approximately 75000 Da higher than the molecular mass estimates of the alliinase molecule as measured by gel-filtration chromatography
220000
-
gel filtration
386000
-
2 stable enzyme forms detected: MW 386000 Da and 580000 Da, gel filtration
580000
-
2 stable enzyme forms detected: MW 386000 Da and 580000 Da, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
-
1 * 52700, alliinase I, SDS-PAGE; 1 * 57500, alliinase II, SDS-PAGE
pentamer
-
SDS-PAGE, two alpha-subunits (68.1 kDa each), one beta-subunit (56.0 kDa), one gamma-subunit (24.8 kDa), and one delta-subunit (13.9 kDa). The two alpha-subunits are connected by a disulfide bridge, and both alpha- and beta-subunits are glycosylated
tetramer
additional information
there are 10 cysteine residues per alliinase monomer, eight of which form four disulfide bridges and two are free thiols. Cys368 and Cys376 form a SAS bridge located near the C-terminal and plays an important role in maintaining both the rigidity of the catalytic domain and the substrate-cofactor relative orientation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-enzyme crystallized in tetragonal form; enzyme crystallized in the presence of S-allyl-L-cysteine, forming dendrite-like monoclinic crystals
-
hanging drop method, crystals are grown under three conditions yielding four different crystal forms. The best diffraction is observed with crystal form IV, space group P2(1)2(1)2(1), a = 68.4, b = 101.1, c = 155.7 A, grown from an ammonium sulfate solution
-
hanging-drop vapour-diffusion method. Crystals belong to space group P2(1) with unit-cell parameters a 0 70.19, b = 127.006, c = 108.085 A, beta = 93.384
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
very unstable below pH 4.5
34630
5 - 10
-
detectable activity
706313
5.5 - 10.5
-
purified enzyme, 4C, completely stable at pH 7.0-9.0, about 50% of maximal activity at pH 5.5 and pH 10.5
728940
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 52
-
alliinase activity increases with increasing temperature over a range of 4.0C to 52C. At 67C, enzyme activity falls precipitously, and at 84C, alliinase activity is completely lost, 10 min, pH 8.0
20 - 45
-
thermostability of the immobilized enzyme is better than that of the free enzyme, especially at high temperature. The free enzyme retains only 5.8% of its original activity following heat treatment at 45C for 3 h, whereas the immobilized enzyme retains 40% of its original activity
20
-
purified native enzyme, loss of 42% activity within 30 min
40 - 60
-
the enzyme is thermolabile und shows loss of activity during the preserving drying process, sugars present in the garlic and the high molecular mass of the enzyme were responsible for protection against degradation at high drying temperatures of 40-60C. The 40-60C drying cyclic with the 4times 20-min sequences preserves 91% of the enzyme activity, compared to 90% and 74% for constant temperatures of 40C and 60C, respectively, degradation mechanism, inactivation at 60C, overview
40 - 50
-
purified native enzyme, loss of 50% activity within 30 min, 40% activity remianing after 30 min at 50C
42
-
purified native enzyme, 30 min, denaturing starts
60
-
purified native enzyme, 30 min, inactivation
additional information
-
low-frequency and low-intensity ultrasound improves the enzyme's thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alliinase is stabilized with 10% glycerol, 0.17 M NaCl and 25 mM pyridoxal-5-phosphate dissolved in phosphate buffer (pH 6.5, 20 mM)
-
alliinase is stabilized with 10% glycerol, 0.17 M NaCl and 25 mM pyridoxal-5-phosphate dissolved in phosphate buffer (pH 6.5, 20 mM), the N-succinyl-chitosan immobilized alliinase retains 85% of its initial activity even after being recycled 5times
-
cycled thawing and freezing leads to a loss in activity of about 40% for each cycle
-
stability of lectin-alliinase complex
the partially purified enzyme can be stabilized over several months by addition of sodium chloride, sucrose, and pyridoxal 5'-phosphate. The stabilized enzyme can be freeze-dried
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C - 4C, purified native enzyme, completely stable for at least 1 week
-
-20C, 10% v/v glycerol, 0.02 mM pyridoxal 5'-phosphate, stable for more than 50 days
-
0-4C, 10% v/v glycerol, 0.02 mM pyridoxal 5'-phosphate, stable for some hours
-
13C, lyophilized preparations retains activity for more than 2 years
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alliin lyase I and alliin lyase II
-
lectin-alliinase complexes do not occur in vivo but are formed in vitro after homogenization of the tissue
native enzyme 300fold to homogeneity by anion exchange, hydrophobic interaction, and aminohexyl affinity chromatography, followed by another different step of anion exchange chromatography and gel filtration
-
native enzyme by gel filtration and lectin concanavalin A affinity chromatography
-
native enzyme from cloves by ammonium sulfate fractionation, dialysis, and gel filtration
-
precipitation with ammonium sulfate, ion-exchange, hydroxyapatite, and gel-filtration chromatographies in sequence
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, Saccharomyces cerevisiae and Pichia pastoris
-
expression in Escherichia coli and Saccharomyces cerevisiae
-
expression in Xenopus leavis oocytes
-
sequence comparison
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K280A
-
almost no detectable alliinase activity
K280R
-
almost no detectable alliinase activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
-
lachrymatory factor synthase and alliinase function in tandem, with the alliinase furnishing the sulfenic acid substrate on which the lachrymatory factor synthase acts. The lachrymatory factor synthase modulates the formation of biologically active thiosulfinates that are downstream of the alliinase in a manner dependent upon the relative concentrations of the lachrymatory factor synthase and the alliinase. These observations suggest that manipulation of lachrymatory factor synthase-to-alliinase ratios in plants displaying this system may provide a means by which to rationally modify organosulfur small molecule profiles to obtain desired flavor and/or odor signatures, or increase the presence of desirable biologically active small molecules
drug development
medicine
pharmacology
synthesis
-
immobilized alliinase in reversibly soluble N-succinyl-chitosan is suitable to catalyze the conversion of alliin to allicin, as active ingredient of pharmaceutical compositions and food additive
additional information