4.1.2.47: (S)-hydroxynitrile lyase
This is an abbreviated version!
For detailed information about (S)-hydroxynitrile lyase, go to the full flat file.
Word Map on EC 4.1.2.47
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4.1.2.47
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esculenta
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manihot
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brasiliensis
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hevea
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synthesis
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cassava
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ketone
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hcn
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lyases
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benzaldehyde
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s-mandelonitrile
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rubber
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athnl
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crantz
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hydrocyanic
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s-cyanohydrins
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r-selective
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arylacetonitrilase
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s-enantiomer
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cyanogenesis
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montanum
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s-mandelic
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pharmacology
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agriculture
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analysis
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drug development
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food industry
- 4.1.2.47
- esculenta
- manihot
- brasiliensis
- hevea
- synthesis
- cassava
- ketone
- hcn
- lyases
- benzaldehyde
-
s-mandelonitrile
- rubber
- athnl
- crantz
-
hydrocyanic
-
s-cyanohydrins
-
r-selective
- arylacetonitrilase
-
s-enantiomer
-
cyanogenesis
- montanum
-
s-mandelic
- pharmacology
- agriculture
- analysis
- drug development
- food industry
Reaction
Synonyms
(R)-LuHNL, (R)-Oxynitrilase, (S)-cyanohydrin producing hydroxynitrile lyase, (S)-Hb-HNL, (S)-HbHNL, (S)-HNL, (S)-Hydroxynitrile lyase, (S)-Me-HNL, (S)-MeHNL, (S)-Oxynitrilase, (S)-selective HNL, (S)-selective hydroxynitrile lyase, Acetone cyanohydrin lyase, ACL, alpha-Hydroxynitrile lyase, EC 4.1.2.37, EC 4.1.2.39, Hb-HNL, HbHNL, HNL, HNL1, Hydroxynitrile lyase, LuHNL, MeHNKL, MeHNL, mut-HNL1, Oxynitrilase, S-HnL, S-hydroxynitrile lyase, S-selective HnL, S-selective hydroxynitrile lyase, S-stereoselective HNL
ECTree
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pH Stability
pH Stability on EC 4.1.2.47 - (S)-hydroxynitrile lyase
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3.5
enzyme is inactivated very fast. Stability decreases with higher buffer concentrations at pH 3.5 in all three buffer systems (phosphate buffer, glutamate buffer, citrate buffer)
705188
6.5
very stable above. At pH 6.5 stability increases with increasing buffer concentration in all three systems (phosphate buffer, glutamate buffer, citrate buffer). The enzyme is most stable in phosphate buffer whereas for glutamate buffer the relative increase of half-life with concentration is more pronounced
705188
decativation below pH 4.0, an unfolding of the enzyme followed by aggregation leading to closely packed enzyme particles at low pH values
703489
4
half-life time: 2 h, the deactivation of the enzyme at slightly acidic pH is a result of pronounced structural unfolding
704762
4
the enzyme shows still 40% of its maximal activity at pH 4.0, while its activity is drastically reduced below pH 4.0
704762
5
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unstable below. Fivefold increase in half-life under optimal conditions by Venoruton and monohydroxyethylrutoside. 50% increase in half-life by 5-20 ng/ml rutin and 1.5-6 ng/ml by hyperoside
655659