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Information on EC 4.4.1.4 - alliin lyase and Organism(s) Allium sativum and UniProt Accession Q41233
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4.4.1.4 alliin lyaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.4.1.4
- garlic
- allium
- allicin
- sativum
- onion
- thiosulfinates
-
crush
- clove
-
organosulfur
-
s-alkenyl-l-cysteine
- alliaceae
- leek
- s-allyl-l-cysteine
-
lachrymatory
- medicine
-
acsos
-
s-allyl
- synthesis
- nutrition
- drug development
- biotechnology
- analysis
- pharmacology
The taxonomic range for the selected organisms is: Allium sativum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alliinase, alliin lyase, cysteine sulfoxide lyase, allinase, alliin-lyase, l-cysteine sulfoxide lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkylcysteine sulfoxide lyase
-
-
-
-
alliinase
cysteine sulfoxide lyase
Cysteine sulphoxide lyase
-
-
-
-
L-cysteine sulfoxide lyase
-
-
-
-
lyase, alliin
-
-
-
-
S-alkyl(en)yl-L-cysteine lyase
-
-
-
-
S-alkylcysteine sulfoxide lyase
-
-
-
-
additional information
the enzyme belongs to the fold-type I family of pyridoxal-5'-phosphate-dependent enzymes
alliinase
-
-
-
-
alliinase
-
-
cysteine sulfoxide lyase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
S-alkyl-L-cysteine S-oxide alkyl-sulfenate-lyase (2-aminoacrylate-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9031-77-0
-
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
(+)-(S)-allyl-L-cysteine sulfoxide
2-propenyl 2-propenethiosulfinate + pyruvate + NH3
-
-
i.e. allicin
-
?
(+)-alliin
allicin + pyruvic acid + NH3
-
isolated from garlic and synthetic substrate (S)-allyl-L-cysteine sulfoxide
i.e. 2-propenyl 2-propenethiosulfinate
-
?
(+)-S-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
-
-
-
-
?
(+/-)-(1-methyl)-L-cysteine sulfoxide
methanesulfenic acid + pyruvate + NH3
-
about 15% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(butyl)-L-cysteine sulfoxide
butane-1-sulfenic acid + pyruvate + NH3
-
6.5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-(propyl)-L-cysteine sulfoxide
propyl-1-sulfenic acid + pyruvate + NH3
-
3.5% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-(2-propenyl)-L-cysteine sulfoxide
2-propene-thioic acid + pyruvate + ammonia
-
about 20% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(-)-alliin
allicin + pyruvic acid + NH3
-
isolated from garlic and synthetic substrate (S)-allyl-L-cysteine sulfoxide
i.e. 2-propenyl 2-propenethiosulfinate
-
?
2 S-ethyl-L-Cys sulfoxide + H2O
ethyl ethanethiosulfinate + 2 pyruvate + 2 NH3
-
-
-
-
?
L-cystine
pyruvate + NH4+ + S2- + L-cysteine
-
cystine lyase activity of the enzyme alliinase
-
-
?
S-(+)-allyl-L-cysteine sulfoxide + H2O
allyl 2-propenethiosulphinate
-
-
-
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
-
-
-
-
?
S-ethyl-L-Cys sulfoxide + H2O
ethylsulfenic acid + pyruvate + NH3
-
about 25% of the activity with (+)-S-(2-propenyl)-L-cysteine sulfoxide
-
-
?
(+/-)-alliin
allicin + pyruvic acid + NH3
-
carbon-sulfur (C-S) bond lyase activity of alliinase and catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibodies, VHHs, overview
-
-
?
(+/-)-alliin
allicin + pyruvic acid + NH3
-
isolated from garlic and synthetic substrate (S)-allyl-L-cysteine sulfoxide
i.e. 2-propenyl 2-propenethiosulfinate
-
?
(+/-)-alliin
allicin + pyruvic acid + NH3
-
rapid, but thermolabil enzyme reaction
-
-
?
2 alliin + H2O
allicin + 2 pyruvate + 2 NH3
-
higher affinity of immobilized enzyme toward its substrate
-
-
?
alliin
allylsulfenic acid + pyruvate + NH3
-
-
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
-
?
additional information
?
-
alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate
-
-
?
additional information
?
-
-
alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
allinase catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic
-
-
?
additional information
?
-
-
cell viability of B16 F10 (B16) cells treated with catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibodies, VHHs, is reduced
-
-
?
additional information
?
-
-
substrate is gained from different garlic sources or synthetically
-
-
?
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
(+)-(S)-allyl-L-cysteine sulfoxide
2-propenyl 2-propenethiosulfinate + pyruvate + NH3
-
-
i.e. allicin
-
?
S-allyl-L-cysteine sulfoxide + H2O
2-propene-thioic acid + pyruvate + NH4+ + H+
-
-
-
-
?
additional information
?
-
alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate
-
-
?
additional information
?
-
-
alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate
-
-
?
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
?
-
-
allinase catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic
-
-
?
additional information
?
-
-
cell viability of B16 F10 (B16) cells treated with catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibodies, VHHs, is reduced
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
contains 1.68 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains one mol of pyridoxal 5'-phosphate per mol of subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
generation and selection, as well as evaluation of variable domain of the heavy chain of a heavy-chain antibodies specific against the alliinase with inhibitory potency against alliinase, inhibitory nanobody VHHA4 that recognizes the active site. Inhibition of B16 F10 cell proliferation by antibody VHH C10 in the presence of alliin, inhibition kinetics, overview
-
additional information
-
alliinase activity decreases with increasing time of treatment with dense phase carbon dioxide as well as higher treatment pressure and temperature
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis of the alliin/alliinase system using a fiber-optic in situ mon-itoring system (fiber-optic drug dissolution test system, FODT) to explore the application of a fiber-opticsensor analysis technique in the process of monitoring catalytic kinetics, method and mathematical modeling, overview
-
1.521
(+/-)-alliin
-
catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C
1.32
4-mercaptopyridine
-
catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C
2.65
L-cystine
-
preparation obtained from garlic powder, activity calculated from the amount of enzymatically formed pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
(+/-)-alliin
-
catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C
0.00185
4-mercaptopyridine
-
catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.331
(+/-)-alliin
-
catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C
0.084
4-mercaptopyridine
-
catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11.4
-
sample treated with dense phase carbon dioxide at 13MPa and 55°C for 60 min, pH 6.5, 25°C
59 - 1003
-
purified catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibodies, pH 7.0, 35°C, substrate (+/-)-alliin
additional information
additional information
activities of native enzyme and S-biotinylated alliinase
additional information
-
activities of native enzyme and S-biotinylated alliinase
additional information
-
the purified alliinase shows an activity of 774.6 U/ml in presence of ultrasound, while its activity reduces to 542.5 U/ml in the absence of ultrasound
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7
-
immobilized alliinase on N-succinyl-chitosan with glutaraldehyde, shifting on the optimum pH of the immobilized alliinase, 25°C
7
-
immobilized alliinase, the optimum pH shifts from 6.0 to 7.0 by the immobilization
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
LITERATURE
35
40
35
-
purified enzyme, optimal temperature of alliinase activity in both the presence and absence of ultrasound, best at 0.4 W cm-2
40
-
immobilized alliinase on N-succinyl-chitosan, shifting on the optimum temperature of the immobilized alliinase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
additional information
-
the enzyme activity declines rapidly at body temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transcription of both cysteine synthase and alliinase is highest during sprouting and decreases significantly in fully developed leaves. Transcriptional activity further declines at the end of the growing season
-
the alliinase gets significantly altered during the drying process of garlic powder
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme alliinase resides in microcompartments separated by thin membranes, and is thus physically kept apart from its substrate alliin
-
additional information
-
the enzyme alliinase resides in microcompartments separated by thin membranes, and is thus physically kept apart from its substrate alliin
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALLN2_ALLSA
473
0
54183
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
-
2 * 42000, gel filtration on a column equilibrated with 6 M urea
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
-
2 * 42000, gel filtration on a column equilibrated with 6 M urea
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
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
LITERATURE
side-chain modification
side-chain modification
-
the enzyme is glycosylated at Asn146 in the sequence Asn146-Met147-Thr148
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
preparation of encapsulated alliinase from Allium sativum in alginate microparticles to improve the use of the enzyme from garlic for medical oral treatments, method, overview. The enzyme activity of the encapsulated enzyme is increased compared to non-encapsulated, especially at low pH
additional information
-
production of antibodies with alliinase activities by exploiting the molecular mimicry of Camelus bactrianus nanobodies: enrichment of variable domain of the heavy chain of a heavy-chain antibodies specific against the alliinase via phage display, recombinant expression of the selected His-tagged antibodies in Escherichia coli strain BL21(DE3), and purification by nickel affinity chromatography
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
strong acidic conditions as well as strong basic conditions result in complete loss of activity
34628
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 45°C 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 40-60°C. The 40-60°C drying cyclic with the 4times 20-min sequences preserves 91% of the enzyme activity, compared to 90% and 74% for constant temperatures of 40°C and 60°C, respectively, degradation mechanism, inactivation at 60°C, overview
50
-
10 min, 10% v/v glycerol, 0.02 mM pyridoxal 5'-phosphate, more than 80% loss of activity
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
-
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
-20°C, 10% v/v glycerol, 0.02 mM pyridoxal 5'-phosphate, stable for more than 50 days
-
0-4°C, 10% v/v glycerol, 0.02 mM pyridoxal 5'-phosphate, stable for some hours
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
-
-
lectin-alliinase complexes do not occur in vivo but are formed in vitro after homogenization of the tissue
-
native enzyme by gel filtration and lectin concanavalin A affinity chromatography
-
native enzyme from cloves by ammonium sulfate fractionation, dialysis, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
nutrition
-
dense phase carbon dioxide has a significant effect on the greening of intact garlic (Allium sativum L.) cloves. The formation of the green colour is a comprehensive result of dense phase carbon dioxide on changing cellular structure, alliin consumption and alliinase activity. DPCD treatment at 10 MPa and 55°C is the optimum condition for the greening of Laba 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
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
analysis
-
development of a qRT-PCR assay that enables the quantification and normalisation of alliinase and cysteine synthase transcripts
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
-
Allium sativum is used as a food, spice, and traditional medicine for many centuries. It has also antibacterial, antioxidant, anticancer and cholesterol-lowering effects, many health benefits associated with garlic can be attributed to thiosulfinates, especially allicin (2-propenyl 2-propenethiosulfinate) generated by the enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nock, L.P.; Mazelis, M.
The C-S lyases of higher plants. Direct comparison of the physical properties of homogeneous alliin lyase of garlic (Allium sativum) and onion (Allium cepa)
Plant Physiol.
85
1079-1083
1987
Allium cepa, Allium sativum
Nock, L.P.; Mazelis, M.
The C-S lyases of higher plants: preparation and properties of homogeneous alliin lyase from garlic (Allium sativum)
Arch. Biochem. Biophys.
249
27-33
1986
Allium sativum
Jansen, H.; Muller, B.; Knobloch, K.
Alliin lyase from garlic, Allium sativum: investigations on enzyme/substrate, enzyme/inhibitor interactions and on a new coenzyme
Planta Med.
55
440-445
1989
Allium sativum
Van Damme, E.J.M.; Smeets, K.; Torrekens, S.; van Leuven, F.; Peumans, W.J.
Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species
Eur. J. Biochem.
209
751-757
1992
Allium cepa var. aggregatum, Allium sativum
Rabinkov, A.; Zhu, X.Z.; Grafi, G.; Galili, G.; Mirelman, D.
Alliin lyase (Alliinase) from garlic (Allium sativum). Biochemical characterization and cDNA cloning
Appl. Biochem. Biotechnol.
48
149-171
1994
Allium sativum
Smeets, K.; van Damme, E.J.M.; van Leuven, F.; Peumans, W.J.
Isolation and characterization of lectins and lectin-alliinase complexes from bulbs of garlic (Allium sativum) and ramsons (Allium ursinum)
Glycoconj. J.
14
331-343
1997
Allium sativum, Allium ursinum
Jansen, H.; Muller, B.; Knobloch, K.
Characterization of an alliin lyase preparation from garlic (Allium sativum)
Planta Med.
55
434-439
1989
Allium sativum
Krest, I.; Keusgen, M.
Stabilization and pharmaceutical use of alliinase
Pharmazie
54
289-293
1999
Allium sativum
Weik, R.; Francky, A.; Striedner, G.; Raspor, P.; Bayer, K.; Mattanovich, D.
Recombinant expression of alliin lyase from garlic (Allium sativum) in bacteria and yeasts
Planta Med.
64
387-389
1998
Allium sativum
Rabinkov, A.; Wilchek, M.; Mirelman, D.
Alliinase (alliin lyase) from garlic (Alliium sativum) is glycosylated at Asn146 and forms a complex with a garlic mannose-specific lectin
Glycoconj. J.
12
690-698
1995
Allium sativum
Krest, I.; Keusgen, M.
Quality of herbal remedies from Allium sativum: differences between alliinase from garlic powder and fresh garlic
Planta Med.
65
139-143
1999
Allium sativum
Shimon, L.J.; Rabinkov, A.; Miron, T.; Mirelman, D.; Wilchek, M.; Frolow, F.
Alliin lyase (alliinase) from garlic (Allium sativum): crystallization and preliminary X-ray characterization
Acta Crystallogr. Sect. D
58
1335-1337
2002
Allium sativum
Kuettner, E.B.; Hilgenfeld, R.; Weiss, M.S.
Purification, characterization, and crystallization of alliinase from garlic
Arch. Biochem. Biophys.
402
192-200
2002
Allium sativum
Jin, Y.N.; Choi, Y.H.; Yang, C.H.
Identification of an essential tryptophan residue in alliinase from garlic (Allium sativum) by chemical modification
Bull. Korean Chem. Soc.
22
68-76
2001
Allium sativum
-
Krest, I.; Glodek, J.; Keusgen, M.
Cysteine sulfoxides and alliinase activity of some Allium species
J. Agric. Food Chem.
48
3753-3760
2000
Allium hymenorrhizum, Allium jesdianum, Allium obliquum, Allium sativum, Allium saxatile, Allium sphaerocephalon, Allium stipitatum, Allium subhirsutum, Allium victorialis
Lawson, L.D.; Wang, Z.J.
Low allicin release from garlic supplements: a major problem due to the sensitivities of alliinase activity
J. Agric. Food Chem.
49
2592-2599
2001
Allium sativum
Yamazaki, M.; Sugiyama, M.; Saito, K.
Intercellular localization of cysteine synthase and alliinase in bundle sheaths of Allium plants
Plant Biotechnol.
19
7-10
2002
Allium cepa, Allium sativum, Allium tuberosum
-
Kao, S.H.; Hsu, C.H.; Su, S.N.; Hor, W.T.; Chang T.W.H.; Chow, L.P.
Identification and immunologic characterization of an allergen, alliin lyase, from garlic (Allium sativum)
J. Allergy Clin. Immunol.
113
161-168
2004
Allium ampeloprasum, Allium cepa, Allium cepa var. aggregatum, Allium sativum
Miron, T.; SivaRaman, H.; Rabinkov, A.; Mirelman, D.; Wilchek, M.
A method for continuous production of allicin using immobilized alliinase
Anal. Biochem.
351
152-154
2006
Allium sativum
Imai, S.; Akita, K.; Tomotake, M.; Sawada, H.
Model studies on precursor system generating blue pigment in onion and garlic
J. Agric. Food Chem.
54
848-852
2006
Allium cepa, Allium sativum
Shimon, L.J.; Rabinkov, A.; Shin, I.; Miron, T.; Mirelman, D.; Wilchek, M.; Frolow, F.
Two structures of alliinase from Alliium sativum L.: apo form and ternary complex with aminoacrylate reaction intermediate covalently bound to the PLP cofactor
J. Mol. Biol.
366
611-625
2007
Allium sativum
Keusgen, M.
Unusual cystine lyase activity of the enzyme alliinase: direct formation of polysulphides
Planta Med.
74
73-79
2008
Allium sativum
Mendez Lagunas, L.L.; Castaigne, F.
Effect of temperature cycling on allinase activity in garlic
Food Chem.
111
56-60
2008
Allium sativum
Weiner, L.; Shin, I.; Shimon, L.J.; Miron, T.; Wilchek, M.; Mirelman, D.; Frolow, F.; Rabinkov, A.
Thiol-disulfide organization in alliin lyase (alliinase) from garlic (Allium sativum)
Protein Sci.
18
196-205
2009
Allium sativum (Q41233), Allium sativum
Zhou, J.
Immobilization of alliinase and its application: Flow-injection enzymatic analysis for alliin
Afr. J. Biotechnol.
8
1337-1342
2009
Allium sativum
-
Appel, E.; Vallon-Eberhard, A.; Rabinkov, A.; Brenner, O.; Shin, I.; Sasson, K.; Shadkchan, Y.; Osherov, N.; Jung, S.; Mirelman, D.
Therapy of murine pulmonary aspergillosis with antibody-alliinase conjugates and alliin
Antimicrob. Agents Chemother.
54
898-906
2010
Allium sativum
Zhou, J.; Wang, J.
Immobilization of alliinase with a water soluble-insoluble reversible N-succinyl-chitosan for allicin production
Enzyme Microb. Technol.
45
299-304
2009
Allium sativum
-
Luo, D.; Guo, J.; Wang, F.; Jin, Z.; Cheng, X.; Zhu, J.; Peng, C.; Zhang, C.
Anti-fungal efficacy of polybutylcyanoacrylate nanoparticles of allicin and comparison with pure allicin
J. Biomat. Sci. Polym. Ed.
20
21-31
2009
Allium sativum
Ko, J.A.; Lee, Y.L.; Jeong, H.J.; Park, H.J.
Preparation of encapsulated alliinase in alginate microparticles
Biotechnol. Lett.
34
515-518
2012
Allium sativum
Li, J.W.; Xia, L.; Su, Y.; Liu, H.; Xia, X.; Lu, Q.; Yang, C.; Reheman, K.
Molecular imprint of enzyme active site by camel nanobodies: rapid and efficient approach to produce abzymes with alliinase activity
J. Biol. Chem.
287
13713-13721
2012
Allium sativum
Zhang, H.; Xiao, W.; Zhao, D.; Liu, Y.; Hu, S.; Chen, C.; Xu, P.; Li, X.; Chen, J.
Fiber-optic in situ analysis of the catalytic kinetics of the alliin/alliinase system
J. Mol. Catal. B
106
111-116
2014
Allium sativum
-
Wang, J.; Cao, Y.; Wang, C.; Sun, B.
Low-frequency and low-intensity ultrasound accelerates alliinase-catalysed synthesis of allicin in freshly crushed garlic
J. Sci. Food Agric.
91
1766-1772
2011
Allium sativum
Mitrova, K.; Svoboda, P.; Milella, L.; Ovesna, J.
Alliinase and cysteine synthase transcription in developing garlic (Allium sativum L.) over time
Food Chem.
251
103-109
2018
Allium sativum
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