Information on EC 4.4.1.4 - alliin lyase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
4.4.1.4
-
RECOMMENDED NAME
GeneOntology No.
alliin lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-elimination
-
-
elimination
-
-
of RSH, C-S bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
alliin degradation
-
ethiin degradation
-
isoalliin degradation
-
SYSTEMATIC NAME
IUBMB Comments
S-alkyl-L-cysteine S-oxide alkyl-sulfenate-lyase (2-aminoacrylate-forming)
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alkylcysteine sulfoxide lyase
-
-
-
-
ALL1
-
-
alliin lyase
-
-
alliinase
-
-
-
-
alliinase
-
-
alliinase
Q41233
-
alliinase
-
-
alliinase
-
-
alliinase I
-
-
alliinase II
-
-
allinase
-
-
allinase
-
-
allinase
Allium tripedale
-
-
allinase
Allium tripedale Trautv.
-
-
-
C-S lyase
-
-
C-S lyase
Allium giganteum Regel
-
-
-
C-S lyase
Q41233
-
C-S-lyase
-
-
cys sulfoxide lyase
-
-
cys sulfoxide lyase
Q41233
-
cysteine sulfoxide lyase
-
-
-
-
cysteine sulfoxide lyase
-
-
Cysteine sulphoxide lyase
-
-
-
-
L-cysteine sulfoxide lyase
-
-
-
-
S-alkyl(en)yl-L-cysteine lyase
-
-
-
-
S-alkylcysteine sulfoxide lyase
-
-
-
-
lyase, alliin
-
-
-
-
additional information
Q41233
the enzyme belongs to the fold-type I family of pyridoxal-5'-phosphate-dependent enzymes
CAS REGISTRY NUMBER
COMMENTARY
9031-77-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
var. Rijnsburger
-
-
Manually annotated by BRENDA team
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
Allium giganteum Regel
-
-
-
Manually annotated by BRENDA team
Allium tripedale
Trautv.
-
-
Manually annotated by BRENDA team
Allium tripedale Trautv.
Trautv.
-
-
Manually annotated by BRENDA team
C-S lyase I and C-S lyase II
-
-
Manually annotated by BRENDA team
Leucocoryne odorata
-
-
-
Manually annotated by BRENDA team
Penicillium corymbiferum
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-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
-
about 10% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(1-methyl)-L-cysteine sulfoxide
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 15% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(1-methyl)-L-cysteine sulfoxide
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 30% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(1-methyl)-L-cysteine sulfoxide
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 35% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(1-methyl)-L-cysteine sulfoxide
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 45% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
6.5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
7% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
8% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 10% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 15% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
3.5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
4% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
7% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 10% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 20% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
-
about 15% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
-
about 20% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
-
about 25% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
-
about 3.5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
show the reaction diagram
-
about 30% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)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
Allium giganteum, Allium giganteum Regel
-
-
precursor of the orange-red pigment formed upon wounding. Two molecules of 2-pyrrolesulfenic acid give rise to highly reactive S-(2-pyrrolyl)2-pyrrolethiosulfinate which in turn converts into red 2,2'-epidithio-3,3'-dipyrrole (dipyrrolo[2,3-d:2',3'-e]-1,2-dithiin)
-
?
(S)-(2-pyrrolyl)cysteine S-oxide
2-pyrrolesulfenic acid + 2-aminoacrylate
show the reaction diagram
Allium giganteum, Allium giganteum Regel
-
-
precursor of the orange-red pigment formed upon wounding. Two molecules of 2-pyrrolesulfenic acid give rise to highly reactive S-(2-pyrrolyl)2-pyrrolethiosulfinate which in turn converts into red 2,2'-epidithio-3,3'-dipyrrole (dipyrrolo[2,3-d:2',3'-e]-1,2-dithiin)
-
?
(S)-(3-pyrrolyl)cysteine S-oxide
3-pyrrolesulfenic acid + 2-aminoacrylate
show the reaction diagram
Allium giganteum, Allium giganteum Regel
-
-
-
-
?
2 alliin + H2O
allicin + 2 pyruvate + 2 NH3
show the reaction diagram
-
-, higher affinity of immobilized enzyme toward its substrate
-
-
?
2-hydroxyethiin 16
(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
-
?
alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
-
i.e. (2R)-3-(allylsulfinyl)-2-aminopropanoic acid
The sulfenic acid condenses with loss of water to form thiosulfinates. The alpha-aminoacrylic acid formed initially subsequently breaks down into pyruvate and ammonia
-
?
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
-
-
-
-
?
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
Allium tripedale
-
-
-
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium altyncolicum
-
about 10% of the activity with L-(+)-isoalliin
-
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium globosum, Allium cepa * Allium saxatile
-
about 15% of the activity with L-(+)-alliin
-
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium oliquum
-
about 15% of the activity with L-(+)-isoalliin
-
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium senescens
-
about 5% of the activity with L-(+)-isoalliin
-
-
?
butiin
butane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium tripedale Trautv.
-
-
-
-
?
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
Allium cepa * Allium globosum, Allium cepa * Allium saxatile
-
about 20% of the activity with L-(+)-alliin
-
-
?
ethiin
ethanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium oliquum, Allium cepa * Allium senescens
-
about 5% of the activity with L-(+)-isoalliin
-
-
?
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
Allium cepa * Allium globosum, Allium cepa * Allium saxatile
-
highest activity
-
-
?
L-(+)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium cepa * Allium oliquum
-
about 35% of the activity with L-(+)-isoalliin
-
-
?
L-(+)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium senescens
-
about 60% of the activity with L-(+)-isoalliin
-
-
?
L-(+)-isoalliin
?
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium oliquum, Allium cepa * Allium senescens
-
highest activity
-
-
?
L-(+)-isoalliin
?
show the reaction diagram
Allium cepa * Allium globosum
-
about 90% of the activity with L-(+)-alliin
-
-
?
L-(+)-isoalliin
?
show the reaction diagram
Allium cepa * Allium saxatile
-
as active as with L-(+)-alliin
-
-
?
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
Allium cepa * Allium oliquum
-
about 15% of the activity with L-(+)-isoalliin
-
-
?
L-(-)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium cepa * Allium altyncolicum
-
about 20% of the activity with L-(+)-isoalliin
-
-
?
L-(-)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium cepa * Allium chevsuricum
-
about 25% of the activity with L-(+)-isoalliin
-
-
?
L-(-)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium senescens
-
about 30% of the activity with L-(+)-isoalliin
-
-
?
L-(-)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium cepa * Allium globosum
-
about 40% of the activity with L-(+)-alliin
-
-
?
L-(-)-alliin
2-propene-thioic acid + pyruvate + NH4+
show the reaction diagram
Allium cepa * Allium saxatile
-
about 55% of the activity with L-(+)-alliin
-
-
?
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-cystine
?
show the reaction diagram
-
-
-
-
?
L-cystine
?
show the reaction diagram
-
4% of the activity with desglutamyl-lentinic acid
-
-
?
L-cystine
pyruvate + NH4+ + S2- + cysteine
show the reaction diagram
-
cystine lyase activity of the enzyme alliinase
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium tripedale
-
-
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium oliquum
-
about 10% of the activity with L-(+)-isoalliin
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium globosum
-
about 30% of the activity with L-(+)-alliin
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium saxatile
-
about 35% of the activity with L-(+)-alliin
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium senescens
-
about 5% of the activity with L-(+)-isoalliin
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium tripedale Trautv.
-
-
-
-
?
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
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
-
-
-
-
?
methiin
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
-
-, i.e. (SS,RC)-Smethylcysteine S-oxide
-
-
?
methiin
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
Allium giganteum Regel
-
-, i.e. (SS,RC)-Smethylcysteine S-oxide
-
-
?
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
Allium cepa * Allium altyncolicum
-
about 10% of the activity with L-(+)-isoalliin
-
-
?
propiin
propane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium cepa * Allium globosum, Allium cepa * Allium saxatile
-
about 15% of the activity with L-(+)-alliin
-
-
?
propiin
propane-1-sulfenic acid + pyruvate + NH3
show the reaction diagram
Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium oliquum, Allium cepa * Allium senescens
-
about 5% of the activity with L-(+)-isoalliin
-
-
?
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
Allium tripedale, Allium tripedale Trautv.
-
primary products resulting from the alliinase reaction of homoisoalliin seem to be highly unstable and are rapidly converted
-
-
?
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
ethylenesulfenic acid + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
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-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
-
-
-
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
-
-
-
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
-
-
-
-
-
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
-
-
-
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
show the reaction diagram
Penicillium corymbiferum
-
i.e. alliin
-
-
?
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
?
show the reaction diagram
-
2% of the activity with desglutamyl-lentinic acid
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys sulfoxide
ethyl ethanethiosulfinate + pyruvate + NH4+
show the reaction diagram
-
5% of the activity with desglutamyl-lentinic acid
-
-
?
S-ethyl-L-Cys sulfoxide
ethylsulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 25% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
S-ethyl-L-Cys sulfoxide
ethylsulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 30% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
S-ethyl-L-Cys sulfoxide
ethylsulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 35% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
S-ethyl-L-Cys sulfoxide
ethylsulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 50% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
S-ethyl-L-Cys sulfoxide
ethylsulfenic acid + pyruvate + NH3
show the reaction diagram
-
about 55% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
S-ethyl-L-Cys sulfoxide
ethanesulfenic acid + pyruvate + NH4+
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
?
show the reaction diagram
-
40% of the activity with S-ethyl-L-Cys sulfoxide
-
-
?
S-methyl-L-Cys sulfoxide
?
show the reaction diagram
-
5% of the activity with desglutamyl-lentinic acid
-
-
?
S-methyl-L-Cys sulfoxide
methanesulfenic acid + pyruvate + NH4
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
?
show the reaction diagram
-
3% of the activity with desglutamyl-lentinic acid
-
-
?
S-propyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
?
S-propyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
?
S-propyl-L-Cys sulfoxide
?
show the reaction diagram
-
-
-
-
?
S-propyl-L-Cys sulfoxide
?
show the reaction diagram
-
5% of the activity with desglutamyl-lentinic acid
-
-
?
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
-
-
-
-
-
methiin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
functions in the sequence of the lenthionine formation from lentinic acid
-
-
-
additional information
?
-
-
the enzyme is responsible for the degradative conversion of S-alk(en)yl-L-Cys sulfoxide to volatile odorous sulfur-containing metabolites
-
-
-
additional information
?
-
-
the enzyme catalyzes the conversion of odorless (+)-S-alk(en)yl-L-cysteine sulfoxides into volatile thiosulfinates
-
-
-
additional information
?
-
-
the enzyme degrades S-alkyl-L-cysteine sulfoxides, causing the characteristic odor of garlic
-
-
-
additional information
?
-
-
no activity with (+/-)-(ethyl)-L-cysteine sulfoxide
-
-
-
additional information
?
-
-
Trp182 is essential for alliinase activity
-
-
-
additional information
?
-
-
3,4-diethyl-1,2,5-trithiane is produced by the action of alliinase in crushed onion
-
-
-
additional information
?
-
Q41233
alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate
-
-
-
additional information
?
-
-
allinase catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic
-
-
-
additional information
?
-
Q41233
the disulfide bridge between Cys368 and Cys376, located near the C-terminal, plays an important role in maintaining both the rigidity of the catalytic domain and the substrate-cofactor relative orientation, but alliinase activity does not require free SH groups
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(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
Allium giganteum, Allium giganteum Regel
-
-
precursor of the orange-red pigment formed upon wounding. Two molecules of 2-pyrrolesulfenic acid give rise to highly reactive S-(2-pyrrolyl)2-pyrrolethiosulfinate which in turn converts into red 2,2'-epidithio-3,3'-dipyrrole (dipyrrolo[2,3-d:2',3'-e]-1,2-dithiin)
-
?
2 alliin + H2O
allicin + 2 pyruvate + 2 NH3
show the reaction diagram
-
-
-
-
?
2-hydroxyethiin 16
(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
Allium tripedale, Allium tripedale Trautv.
-
-
-
-
?
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 + pyruvate + NH3
show the reaction diagram
Allium tripedale
-
-
-
-
?
methiin
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
-
-
-
-
?
methiin
methanesulfenic acid + 2-aminoacrylate
show the reaction diagram
Allium giganteum, Allium giganteum Regel
-
-
-
-
?
methiin
methanesulfenic acid + pyruvate + NH3
show the reaction diagram
Allium tripedale Trautv.
-
-
-
-
?
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
Allium tripedale, Allium tripedale Trautv.
-
primary products resulting from the alliinase reaction of homoisoalliin seem to be highly unstable and are rapidly converted
-
-
?
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
-
-
-
-
-
methiin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
functions in the sequence of the lenthionine formation from lentinic acid
-
-
-
additional information
?
-
-
the enzyme is responsible for the degradative conversion of S-alk(en)yl-L-Cys sulfoxide to volatile odorous sulfur-containing metabolites
-
-
-
additional information
?
-
-
the enzyme catalyzes the conversion of odorless (+)-S-alk(en)yl-L-cysteine sulfoxides into volatile thiosulfinates
-
-
-
additional information
?
-
-
the enzyme degrades S-alkyl-L-cysteine sulfoxides, causing the characteristic odor of garlic
-
-
-
additional information
?
-
-
3,4-diethyl-1,2,5-trithiane is produced by the action of alliinase in crushed onion
-
-
-
additional information
?
-
Q41233
alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate
-
-
-
additional information
?
-
-
allinase catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate; Lys285 is the pyridoxal phosphate binding site
pyridoxal 5'-phosphate
-
contains 3 mol of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
contains 3.76 mol of pyridoxal 5'-phosphate per mol of enzyme; enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
contains 1.68 mol of pyridoxal 5'-phosphate per mol of enzyme; enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
contains one mol of pyridoxal 5'-phosphate per mol of subunit; enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
stimulates
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Aminooxyacetate
-
-
Dicyclohexylcarbodiimide
-
-
DL-homocysteine
-
competitive
hydrazine
-
-
hydroxylamine
-
completely reversed by pyridoxal 5'-phosphate
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
-
complete loss of enzyme activity
iodoacetate
-
-
L-Cys
-
competitive
N-acetyl-L-Cys
-
competitive
N-Acetylimidazole
-
slightly decreases activity
N-bromosuccinimide
-
rapidly and completely inactivates
Phenylmercury acetate
-
-
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
L-cysteine ethyl ester
-
competitive
additional information
-
inactivation is a result of substrate cleavage, but non of the end products are inhibitors of the enzyme. The inhibition is caused by an unstable precursor of pyruvate
-
additional information
-
microwave inactivation of the enzyme alliinase
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.42
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
0.47
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
0.68
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
0.77
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
0.85
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
1.25
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
1.48
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
1.59
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
1.79
-
(+)-S-(2-propenyl)-L-cysteine sulfoxide
-
pH 7.0, 25C
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
2.9
-
alliin
-
pH 6.5
4.22
-
alliin
-
pH 8.0, 22C
2.2
-
cystine
-
alliinase I
9.7
-
cystine
-
alliinase II
0.06
-
desglutamyl-lentinic acid
-
-
0.88
-
L-(+)-alliin
Allium cepa * Allium saxatile
-
-
1.04
-
L-(+)-alliin
Allium cepa * Allium globosum
-
-
1.44
-
L-(+)-alliin
Allium altyncolicum, Allium cepa * Allium senescens
-
-
1.6
-
L-(+)-alliin
-
enzyme from garlic powder
1.92
-
L-(+)-alliin
Allium cepa * Allium oliquum
-
-
2.33
-
L-(+)-alliin
Allium cepa * Allium chevsuricum
-
-
3.08
-
L-(+)-alliin
Allium cepa * Allium altyncolicum
-
-
2.8
-
L-(-)-alliin
-
enzyme from garlic powder
1.94
-
L-cystine
-
homogenous alliinase prepared from fresh garlic cloves
2.65
-
L-cystine
-
preparation obtained from garlic powder, activity calculated from the amount of enzymatically formed pyruvate
0.39
-
petiveriin
-
pH 8.0, 22C
0.25
-
propiin
-
pH 8.0, 22C
0.4
-
S-(2-chloro-4-nitrophenyl)-L-Cys
-
alliin lyase II
0.5
-
S-(2-chloro-4-nitrophenyl)-L-Cys
-
alliin lyase I
0.4
-
S-(2-chloro-6-nitrophenyl)-L-Cys
-
alliin lyase II
0.7
-
S-(2-chloro-6-nitrophenyl)-L-Cys
-
alliin lyase I
1.1
-
S-allyl-L-Cys sulfoxide
-
-
2.2
-
S-allyl-L-Cys sulfoxide
-
-
3.3
-
S-allyl-L-Cys sulfoxide
-
-
5.8
-
S-allyl-L-Cys sulfoxide
Penicillium corymbiferum
-
-
10
-
S-allyl-L-Cys sulfoxide
-
alliin lyase I
10
-
S-allyl-L-Cys sulfoxide
-
-
11
-
S-allyl-L-Cys sulfoxide
-
alliin lyase II
18.3
-
S-allyl-L-Cys sulfoxide
-
alliinase I
24.1
-
S-allyl-L-Cys sulfoxide
-
alliinase II
2.5
-
S-ethyl-L-Cys sulfoxide
-
-
2.7
-
S-ethyl-L-Cys sulfoxide
-
-
4.2
-
S-ethyl-L-Cys sulfoxide
-
-
4.9
-
S-ethyl-L-Cys sulfoxide
-
-
5.7
-
S-ethyl-L-Cys sulfoxide
-
-
5.8
-
S-ethyl-L-Cys sulfoxide
-
-
13
-
S-ethyl-L-Cys sulfoxide
-
-
16
-
S-ethyl-L-Cys sulfoxide
-
alliin lyase I
24
-
S-ethyl-L-Cys sulfoxide
-
alliin lyase II
45.7
-
S-ethyl-L-Cys sulfoxide
-
alliinase I
68.4
-
S-ethyl-L-Cys sulfoxide
-
alliinase II
47
-
S-methyl-L-Cys sulfoxide
-
alliinase I
55
-
S-methyl-L-Cys sulfoxide
-
-
96.6
-
S-methyl-L-Cys sulfoxide
-
alliinase II
7.6
-
S-phenyl-L-Cys sulfoxide
-
alliin lyase I
9.9
-
S-phenyl-L-Cys sulfoxide
-
alliin lyase II
2.6
-
S-propenyl-L-Cys sulfoxide
-
alliinase I
3
-
S-propenyl-L-Cys sulfoxide
-
alliinase II
0.6
-
S-propyl-L-Cys sulfoxide
-
alliin lyase I
1.1
-
S-propyl-L-Cys sulfoxide
-
-
2.1
-
S-propyl-L-Cys sulfoxide
-
alliin lyase II
16.3
-
S-propyl-L-Cys sulfoxide
-
alliinase II
22
-
S-propyl-L-Cys sulfoxide
-
alliinase I
13.9
-
methiin
-
pH 8.0, 22C
additional information
-
additional information
-
Km and Vmax vary as a function of substrate structure, with the most preferred substrates being the naturally occurring Petiveria alliacea compounds S-benzyl-L-cysteine sulfoxide and S-2-hydroxyethyl-L-cysteine sulfoxide
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8.18
-
(2R)-2-amino-3-(1-phenylethylsulfinyl)propanoic acid
-
pH 8.0, 22C
14.33
-
(2R)-2-amino-3-(2-methylbenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
10.65
-
(2R)-2-amino-3-(4-chlorobenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
2.67
-
(2R)-2-amino-3-(4-methylbenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
2.48
-
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid
-
pH 8.0, 22C
1.75
-
(2R)-2-amino-3-(phenethylsulfinyl)propanoic acid
-
pH 8.0, 22C
6.48
-
(2R)-2-amino-3-(phenylsulfinyl)propanoic acid
-
pH 8.0, 22C
4.2
-
2-hydroxyethiin
-
pH 8.0, 22C
20.67
-
alliin
-
pH 8.0, 22C
15.1
-
methiin
-
pH 8.0, 22C
4.47
-
petiveriin
-
pH 8.0, 22C
1.96
-
propiin
-
pH 8.0, 22C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.49
-
(2R)-2-amino-3-(1-phenylethylsulfinyl)propanoic acid
-
pH 8.0, 22C
289183
13.4
-
(2R)-2-amino-3-(2-methylbenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
289184
44
-
(2R)-2-amino-3-(4-chlorobenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
289188
32.3
-
(2R)-2-amino-3-(4-methylbenzylsulfinyl)propanoic acid
-
pH 8.0, 22C
289186
65.7
-
(2R)-2-amino-3-(ethylsulfinyl)propanoic acid
-
pH 8.0, 22C
289201
66.5
-
(2R)-2-amino-3-(phenethylsulfinyl)propanoic acid
-
pH 8.0, 22C
289193
28.9
-
(2R)-2-amino-3-(phenylsulfinyl)propanoic acid
-
pH 8.0, 22C
289191
73.4
-
2-hydroxyethiin
-
pH 8.0, 22C
293332
42.8
-
alliin
-
pH 8.0, 22C
214243
1.09
-
methiin
-
pH 8.0, 22C
215231
100
-
petiveriin
-
pH 8.0, 22C
293331
68.8
-
propiin
-
pH 8.0, 22C
215366
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.5
-
Trinitrobenzenesulfonic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.17
-
Penicillium corymbiferum
-
-
23.2
-
-
-
109
-
-
-
119.7
-
-
-
126
-
-
-
129.9
-
-
enzyme from garlic powder
152.8
-
-
-
260
-
-
-
490
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q41233
activities of native enzyme and S-biotinylated alliinase
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
free alliinase, 25C
6.5
7
-
sodium phosphate buffer
6.5
-
Penicillium corymbiferum
-
-
6.5
-
Allium cepa * Allium saxatile
-
-
6.5
-
-
optimal for soluble and entrapped alliinase activity
6.5
-
Q41233
assay at
7
8
-
enzyme from garlic powder
7
-
Allium altyncolicum, Allium cepa * Allium senescens
-
-
7
-
-
immobilized alliinase, the optimum pH shifts from 6.0 to 7.0 by the immobilization
7
-
-
immobilized alliinase on N-succinyl-chitosan with glutaraldehyde, shifting on the optimum pH of the immobilized alliinase, 25C
7.4
8.5
-
-
7.4
-
-
potassium phosphate buffer
7.5
-
Allium cepa * Allium altyncolicum, Allium cepa * Allium chevsuricum, Allium cepa * Allium globosum, Allium cepa * Allium oliquum
-
-
8
8.5
-
Tris/HCl buffer
8.1
-
-
Tris-HCl buffer
8.6
-
-
sodium diphosphate buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
7
-
immobilized alliinase
5
10
-
active in the range
5
8
Allium cepa * Allium oliquum
-
about 50% of maximal activity at pH 6.5 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
7.5
Allium cepa * Allium saxatile
-
about 50% of maximal activity at pH 6.5 and 8.0
5.5
8
Penicillium corymbiferum
-
about 20% of maximal activity at pH 5.5 and pH 8.0
5.5
8
-
half-maximal activity at pH 5.5 and at pH 8.0
5.5
8
-
about 50% of maximal activity at pH 6.0 and 8.0
5.5
8
Allium cepa * Allium globosum
-
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
-
half-maximal activity at pH 5.5 and at pH 8.5
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
-
half-maximal activity at pH 6.5 and at pH 8.5
7
11
-
pH 7.0: about 30% of maximal activity, pH 11.0: about 60% of maximal activity
7
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
Q41233
assay at
30
35
-
-
30
-
-
-
30
-
-
free alliinase
34
-
Allium cepa * Allium altyncolicum
-
-
35
-
-
immobilized alliinase, the temperature optimum shifts from 30C to 35C
36
-
-
enzyme from garlic powder
36
-
Allium altyncolicum, Allium cepa * Allium saxatile, Allium cepa * Allium senescens
-
-
38
-
Allium cepa * Allium oliquum
-
-
40
-
Allium cepa * Allium chevsuricum, Allium cepa * Allium globosum
-
-
40
-
-
immobilized alliinase on N-succinyl-chitosan, shifting on the optimum temperature of the immobilized alliinase
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
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
60
-
no activity at 0C, highly reduced activity at 60C, maximal activity at 30C
20
50
-
immobilized alliinase
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Leucocoryne odorata
-
only in
Manually annotated by BRENDA team
-
the alliinase gets significantly altered during the drying process of garlic powder
Manually annotated by BRENDA team
-
alliinase and lectin are the predominant proteins in nectar
Manually annotated by BRENDA team
-
only in
Manually annotated by BRENDA team
Penicillium corymbiferum
-
-
Manually annotated by BRENDA team
-
observation of the reverse transcriptase polymerase chain reaction product
Manually annotated by BRENDA team
-
the enzyme predominantly accumulates in the bundle sheath cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
alliinase and alkyl cysteine sulfoxides are prevented from acting in the intact protoplast by compartimentation of the alliinase in the vacuoles and alkyl cysteine sulfoxides in the cytoplasm
Manually annotated by BRENDA team
-
compartmentalized in plant cell vacuoles, while its substrates, S-alk(en)yl-L-Cys sulfoxides, are located in the cytoplasm
Manually annotated by BRENDA team
additional information
Q41233
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
51000
-
-
alliinase I, gel filtration
57500
-
-
alliinase II, gel filtration
67000
-
-
gel filtration
85000
-
-
gel filtration
90000
-
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 51000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 48000, SDS-PAGE; x * 54083, calculation from nucleotide sequence
dimer
-
2 * 42000, gel filtration on a column equilibrated with 6 M urea
dimer
-
2 * 51400, SDS-PAGE
dimer
-
2 * 52000-54000, SDS-PAGE
dimer
-
1 * 53000 + 1 * 54000, enzyme from garlic powder, SDS-PAGE
dimer
Q41233
homodimer
homodimer
-
two equal subunits of 448 amino acid residues
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
-
4 * 50000, gel filtration on a column equilibrated with 6 M urea and 0.1% SDS
tetramer
-
4 * 52000, SDS-PAGE
monomer
-
1 * 52700, alliinase I, SDS-PAGE; 1 * 57500, alliinase II, SDS-PAGE
additional information
Q41233
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 ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
glycoprotein; major sugars are mannose, glucose and galactose
glycoprotein
-
alliinase I and alliinase II differ in glycosylation. Both contain xylose/fucose containing complex-type N-linked glycans, and alliinase II also contains terminal mannose structures
side-chain modification
-
glycoprotein; the carbohydrate moiety is 5.8% of the total protein MW, 1.5% hexosamine and 0.5% methylpentose
side-chain modification
-
glycoprotein
side-chain modification
-
glycoprotein
glycoprotein
-
-
side-chain modification
-
contains 5.5% carbohydrate, 40% as pentose; glycoprotein
side-chain modification
-
contains 6% carbohydrate; glycoprotein
side-chain modification
-
glycoprotein; the enzyme is glycosylated at Asn146 in the sequence Asn146-Met147-Thr148
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
very unstable below pH 4.5
5
10
-
detectable activity
6.5
-
-
most stable around
6.5
-
-
strong acidic conditions as well as strong basic conditions result in complete loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
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
50
-
-
30 min, stable in presence of pyridoxal 5'-phosphate
50
-
-
10 min, 10% v/v glycerol, 0.02 mM pyridoxal 5'-phosphate, more than 80% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
stability of lectin-alliinase complex
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
13C, lyophilized preparations retains activity for more than 2 years
-
-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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
lectin-alliinase complexes do not occur in vivo but are formed in vitro after homogenization of the tissue
-
-
Penicillium corymbiferum
-
precipitation with ammonium sulfate, ion-exchange, hydroxyapatite, and gel-filtration chromatographies in sequence
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli, Saccharomyces cerevisiae and Pichia pastoris
-
expression in Xenopus leavis oocytes
-
sequence comparison
Q41233
expression in Escherichia coli and Saccharomyces cerevisiae
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K280A
-
almost no detectable alliinase activity
K280R
-
almost no detectable alliinase activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
major allergen of garlic
analysis
-
microwave inactivation of the enzyme alliinase, to eliminate the interference from alliinase sulfo products, is used for a rapid detection method for determination of herbicides in onions, overview
medicine
-
major allergen of garlic
medicine
-
a chemical conjugate between daidzein and the enzyme alliinase specifically binds to ovarian cancer cells and upon addition of the prodrug alliin, effectively produces cytotoxic allicin molecules which kill the cancer cells. Tumors show a five fold higher uptake as compared to other tissues. Treatment of tumor bearing mice with daidzein-alliinase and alliin effectively attenuates tumor progression during the first 12 days while a 5-fold increase in bioluminescence is detected in placebo-treated animals. Autopsy revealed only small individual foci of luminescence at the site of tumor cells inoculation. Histological examination of organs and tissues did not reveal any additional foci of carcinoma or signs of toxicity
medicine
-
major allergen of garlic
analysis
-
Flow-injection enzymatic analytical system for determination of alliin based on the immobilized alliinase and an ammonia gas electrode provids linearity in the 1 10-5 to 1 10-3 mol/l alliin concentration range and exhibited good repeatability and operational stability
drug development
-
a monoclonal antibody (MAb) against Aspergillus fumigatus is produced and chemically ligated to the enzyme alliinase. The purified antibody-alliinase conjugate binds to conidia and hyphae of Aspergillus fumigatus at nanomolar concentrations. In the presence of alliin, the conjugate produces cytotoxic allicin molecules, which kills the fungus
drug development
-
Pure allicin is prepared by reacting synthetic alliin with a stabilized process of the garlic enzyme alliinase. A novel drug vector, polybutylcyanoacrylate (PBCA) nanoparticles has been developed by emulsion polymerization method and wrapps the pure allicin into it. Minimal inhibitory fungal concentration (MIC) and minimal fungicidal concentration (MFC) of pure allicin and PBCA-allicin NPs against six fungus strains (Candida albicans, Cryputococcus neoformans, Trichophyton rubum, Microsporum gypseum, Microsporum canis and Epidermophyton floccosum) in vitro are used to evaluate their anti-fungal efficacy
medicine
-
no clinical trial should be conducted with a garlic powder supplement that is not standardized upon dissolution allicin release for an effect of garlic that may be related to allicin, as most are
medicine
-
major allergen of garlic
pharmacology
-
allicin contributes to the prevention of stroke and arteriosclerosis. An acid resistant capsule is filled with pellets of alliin and alliinase. In the intestine, alliin and alliinase are dissolved and alicin is liberated
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
pharmacology
-
a triggered antimicrobial system based on different sulfoxide substrates and alliinase might be superior to the application of conventional fungicides or allicin itself
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