4.4.1.4: alliin lyase
This is an abbreviated version!
For detailed information about alliin lyase, go to the full flat file.
Word Map on EC 4.4.1.4
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4.4.1.4
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garlic
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allium
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allicin
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sativum
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onion
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thiosulfinates
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crush
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clove
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organosulfur
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s-alkenyl-l-cysteine
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alliaceae
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leek
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s-allyl-l-cysteine
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lachrymatory
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medicine
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acsos
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s-allyl
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synthesis
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nutrition
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drug development
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biotechnology
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analysis
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pharmacology
- 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
Reaction
Synonyms
alkylcysteine sulfoxide lyase, alkylsulphenate lyase, ALL1, alliin lyase, alliin-lyase, alliinase, alliinase I, alliinase II, allinase, C-S lyase, C-S-lyase, cys sulfoxide lyase, cysteine sulfoxide lyase, Cysteine sulphoxide lyase, L-(+)-S-alk(en)ylcysteine sulfoxide lyase, L-cysteine sulfoxide lyase, lyase, alliin, More, P-19486 alliinase, S-alkyl(en)yl-L-cysteine lyase, S-alkylcysteine sulfoxide lyase
ECTree
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Engineering
Engineering on EC 4.4.1.4 - alliin lyase
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C115A
mutation leads to a decrease of the catalytic efficiency in the gamma-elimination reaction of the physiological substrate by more than an order of magnitude, reation of EC 4.4.1.11
C115H
additional information
mutant cleaves S-alk(en)yl-L-cysteine sulfoxides more effectively than the wild type
C115H
mutation leads to loss of activity in the gamma-elimination reaction of the physiological substrate, reaction of EC 4.4.1.11. The catalytic efficiency in the beta-elimination reaction of S-substituted L-cysteine sulfoxides is increased by about an order of magnitude compared to the wild type
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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
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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