Any feedback?
Information on EC 4.1.2.10 - (R)-mandelonitrile lyase and Organism(s) Prunus dulcis and UniProt Accession O24243
for references in articles please use BRENDA:EC4.1.2.10Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.1.2.10 (R)-mandelonitrile lyaseIUBMB Comments
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
Specify your search results
Word Map
- 4.1.2.10
- cyanohydrin
- prunus
- synthesis
- hcn
- cherry
-
enantioselective
- serotina
- lyases
-
r-mandelonitrile
-
enantiomeric
- amygdalus
-
diisopropyl
- prunasin
-
cyanogenesis
- hbhnl
-
hydrocyanic
-
hevea
-
s-selective
- pharmacology
- agriculture
The taxonomic range for the selected organisms is: Prunus dulcis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mandelonitrile lyase, athnl, (r)-oxynitrilase, (r)-(+)-mandelonitrile lyase, pahnl5, aphnl, r-selective hnl, pahnl1, acix9_0562, (r)-hydroxynitrile lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-(+)-Mandelonitrile lyase
-
-
-
-
(R)-Mandelonitrile lyase
-
-
-
-
(R)-Oxynitrilase
D-alpha-hydroxynitrile lyase
-
-
-
-
D-Hydroxynitrile lyase
-
-
-
-
D-Oxynitrilase
-
-
-
-
Hydroxynitrile lyase
Lyase, mandelonitrile
-
-
-
-
MDL
-
-
-
-
Oxynitrilase
PaHNL5
PhaMDL
-
-
-
-
(R)-Oxynitrilase
-
-
-
-
Hydroxynitrile lyase
-
-
-
-
Oxynitrilase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-mandelonitrile = cyanide + benzaldehyde
based on the binding geometry, a reaction mechanism is proposed that involves one of the two conserved active site histidine residues acting as a general base abstracting the proton from the cyanohydrin hydroxyl group. Site-directed mutagenesis shows that both active site histidines are required for the reaction to occur
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyanohydrin formation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(R)-mandelonitrile benzaldehyde-lyase (cyanide-forming)
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
CAS REGISTRY NUMBER
COMMENTARY
9024-43-5
-
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
cyanide + butanal
(2R)-2-hydroxypentanenitrile
-
100% yield, 90% enantiomeric excess
-
?
cyanide + thiophene-2-carbaldehyde
(2R)-hydroxy(thiophen-2-yl)ethanenitrile
-
48% yield, 87% enantiomeric excess
-
?
2-chlorobenzaldehyde + HCN
(R)-2-chloromandelonitrile
-
-
after 96 h, 100% yield, 21% enantiomeric excess
-
?
3,4-dihydroxybenzaldehyde + HCN
(R)-3,4-dihydroxymandelonitrile
-
-
after 96 h, 100% yield, 99% enantiomeric excess
-
?
3-phenylpropionaldehyde + HCN
(R)-2-hydroxy-4-phenylbutyronitrile
-
-
after 96 h, 83% yield, 91% enantiomeric excess
-
?
4-bromobenzaldehyde + HCN
(R)-4-bromomandelonitrile
-
-
after 96 h, 100% yield, 99% enantiomeric excess
-
?
4-fluorobenzaldehyde + HCN
(R)-4-fluoromandelonitrile
-
-
after 96 h, 100% yield, 72% enantiomeric excess
-
?
4-nitrobenzaldehyde + HCN
(R)-4-nitromandelonitrile
-
-
after 96 h, 100% yield, 14% enantiomeric excess
-
?
benzaldehyde + HCN
(R)-mandelonitrile
-
-
after 96 h, 100% yield, 99% enantiomeric excess
-
?
cyanide + (4R)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde is converted to 47.1% (2S)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 52.9% (2R)-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
?
cyanide + (4R,5S)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-hydroxy-[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile + (2R)-hydroxy-[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R,5S)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde is converted to 34.2% (2S)-hydroxy[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 65.8% (2R)-hydroxy[(4S,5S)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
-
?
cyanide + (4R,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4R,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde is converted to 48.2% (2S)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 51.8% (2R)-[(4S,5S)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
?
cyanide + (4S)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde is converted to 66.4% (2S)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 33.6% (2R)-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
?
cyanide + (4S,5R)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde
(2S)-hydroxy-[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile + (2R)-hydroxy-[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S,5R)-2,2,5-trimethyl-1,3-dioxolane-4-carbaldehyde is converted to 52.6% (2S)-hydroxy[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile and 47.4% (2R)-hydroxy[(4R,5R)-2,2,5-trimethyl-1,3-dioxolan-4-yl]ethanenitrile
-
?
cyanide + (4S,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde
(2S)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile + (2R)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate (4S,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolane-4-carbaldehyde is converted to 49.3% (2S)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile and 50.7% (2R)-[(4R,5R)-2,2-dimethyl-5-phenyl-1,3-dioxolan-4-yl](hydroxy)ethanenitrile
-
?
cyanide + (benzyloxy)acetaldehyde
(2R)-3-(benzyloxy)-2-hydroxypropanenitrile + (2S)-3-(benzyloxy)-2-hydroxypropanenitrile
-
-
43.9% (2S)-3-(benzyloxy)-2-hydroxypropanenitrile and 53.1% (2S)-3-(benzyloxy)-2-hydroxypropanenitrile
-
?
cyanide + (R)-4-methylsulfanylbenzaldehyde
(R)-4-methylsulfanyl-mandelonitrile
-
-
-
-
?
cyanide + 1,4-dioxaspiro[4.5]decane-2-carbaldehyde
(S)-2-hydroxy-2-((R)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile + (R)-2-hydroxy-2-((R)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile + (S)-2-hydroxy-2-((S)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile + (R)-2-hydroxy-2-((S)-1,4-dioxaspiro[4.5]decan-2-yl)acetonitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate 1,4-dioxaspiro[4.5]decane-2-carbaldehyde is converted to 21.8% (2S)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 28.3% (2R)-(2R)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile, 30.3% (2S)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile and 19.6% (2R)-(2S)-1,4-dioxaspiro[4.5]dec-2-yl(hydroxy)ethanenitrile
-
?
cyanide + 2,3,4a,8a-tetrahydro-1,4-benzodioxine-6-carbaldehyde
(2R)-hydroxy(2,3,4a,8a-tetrahydro-1,4-benzodioxin-6-yl)acetonitrile
-
isoenzyme HNL5
-
-
?
cyanide + 2-(benzyloxy)-3-phenylpropanal
(2S,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile + (2R,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile + (2S,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile + (2R,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile
-
-
26.9% (2S,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile, 23.4% (2R,3S)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile, 29.2% (2S,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile and 20.6% (2R,3R)-3-(benzyloxy)-2-hydroxy-4-phenylbutanenitrile
-
?
cyanide + 2-(benzyloxy)propanal
(2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile + (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile + (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile + (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile
-
-
45.4% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile, 8.1% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile, 33.3% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile and 13.3% (2S,3S)-3-(benzyloxy)-2-hydroxybutanenitrile
-
?
cyanide + 2-(naphthalen-2-yl)propanal
(2S,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile + (2S,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile + (2R,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile + (2R,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile
-
-
30.4% (2S,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile, 24.0% (2S,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile, 20.0% (2R,3S)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile and 25.6% (2R,3R)-2-hydroxy-3-(naphthalen-2-yl)butanenitrile
-
?
cyanide + 2-chlorobenzaldehyde
(2R)-(2-chlorophenyl)(hydroxy)ethanenitrile
-
-
15.8% yield and 66% enantiomeric excess after 2 h
-
?
cyanide + 2-methoxy-3-phenylpropanal
(2S,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile + (2R,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile + (2S,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile + (2R,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile
-
-
43.1% (2S,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile, 8.4 (2R,3S)-2-hydroxy-3-methoxy-4-phenylbutanenitrile, 40.1% (2S,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile and 8.4% (2R,3R)-2-hydroxy-3-methoxy-4-phenylbutanenitrile
-
?
cyanide + 2-phenylpropanal
(2R,3S)-2-hydroxy-3-phenylbutanenitrile + (2S,3R)-2-hydroxy-3-phenylbutanenitrile + (2R,3R)-2-hydroxy-3-phenylbutanenitrile
-
-
3.0% (2S,3S)-2-hydroxy-3-phenylbutanenitrile, 51.8% (2R,3S)-2-hydroxy-3-phenylbutanenitrile, 27.6% (2S,3R)-2-hydroxy-3-phenylbutanenitrile and + 17.6% (2R,3R)-2-hydroxy-3-phenylbutanenitrile
-
?
cyanide + 3,4-dihydro-1H-isochromene-3-carbaldehyde
(S)-2-hydroxy-2-((S)-isochroman-3-yl)acetonitrile + (S)-2-hydroxy-2-((R)-isochroman-3-yl)acetonitrile + (R)-2-hydroxy-2-((S)-isochroman-3-yl)acetonitrile + (R)-2-hydroxy-2-((R)-isochroman-3-yl)acetonitrile
-
-
28.6% (2S)-(3S)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile, 21.5% (2R)-(3S)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile, 28.7% (2S)-(3R)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile and 21.1% (2R)-(3R)-3,4-dihydro-1H-isochromen-3-yl(hydroxy)ethanenitrile
-
?
cyanide + 3,4-dihydroxybenzaldehyde
(R)-3,4-dihydroxymandelonitrile
-
synthesis of (R)-3,4-dihydroxymandelonitrile with a yield of 100% and an enantiomeric excess of 99%
-
-
?
cyanide + 3-hydroxy-2,2-dimethylpropanal
(2R)-2,5-dihydroxy-3,3-dimethylpentanenitrile
-
i.e. hydroxypivaldehyde
best enantiomeric excess is obtained at pH 2.5
-
?
cyanide + 3-methoxy-3-phenylpropanal
(2S,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile + (2R,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile + (2S,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile + (2R,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile
-
-
6.5% (2S,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 45.2% (2R,4S)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 14.0% (2S,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile, 34.3% (2R,4R)-2-hydroxy-4-methoxy-4-phenylbutanenitrile
-
?
cyanide + 3-phenoxypropanal
(2R)-2-hydroxy-5-phenylpentanenitrile
-
-
74.3% (2R)-2-hydroxy-5-phenylpentanenitrile and 25.7% (2S)-2-hydroxy-5-phenylpentanenitrile
-
?
cyanide + 3-phenylpropanal
(R)-2-hydroxy-4-phenylbutyronitrile
-
isoenzyme HNL5
-
-
?
cyanide + 3-phenylpropionaldehyde
(R)-2-hydroxy-4-phenyl butyronitrile
-
synthesis of (R)-2-hydroxy-4-phenyl butyronitrile with a yield of 83% and an enantiomeric excess of 91%
-
-
?
cyanide + 3-tetrahydrothiophenone
(S)-3-hydroxytetrahydrothiophene-3-carbonitrile
-
the enzyme, that shows (R)-stereospecificity for its natural substrate shows S-stereselectivity with the heterocyclic ketone as substrate
-
-
?
cyanide + 4-bromoacetophenone
4-bromo-2-hydroxyphenylpropionitrile
-
(R)-cyanohydrin is formed with 5% yield and 99% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-bromobenzaldehyde
(R)-4-bromomandelonitrile
-
synthesis of (R)-4-bromomandelonitrile with a yield pf 100% and an enantiomeric excess value of 99%
-
-
?
cyanide + 4-chloroacetophenone
4-chloro-2-hydroxyphenylpropionitrile
-
(R)-cyanohydrin is formed with 11% yield and 95% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-fluoroacetophenone
4-fluoro-2-hydroxyphenylpropionitrile
-
(R)-cyanohydrin is formed with 20% yield and 84% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-hydroxybenzaldehyde
(R)-4-hydroxymandelonitrile
-
(R)-cyanohydrin is formed with 2% yield and 25% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-hydroxybutanal
(R)-2,5-dihydroxypentanenitrile
-
by varying the different reaction parameters it is possible to reduce the extension of the undesirable non-enzymatic competing reactions and optimize the optical purity of the cyanohydrin product. Best results are obtained at 15°C
-
-
?
cyanide + 4-iodoacetophenone
4-iodo-2-hydroxyphenylpropionitrile
-
(R)-cyanohydrin is formed with 3% yield and 24% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-methoxybenzaldehyde
(2R)-(4-methoxyphenyl)(hydroxy)ethanenitrile
-
(R)-cyanohydrin is formed with 95% yield and 95% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-methyl benzaldehyde
(2R)-(4-methylphenyl)(hydroxy)ethanenitrile
-
(R)-cyanohydrin is formed with 85% yield and 79% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + 4-nitrobenzaldehyde
(R)-4-nitromandelonitrile
-
synthesis of (R)-4-nitromandelonitrile with a yield of 100% and an enantiomeric excess value of 14%
-
-
?
cyanide + 4-phenylbutanal
(2R)-2-hydroxy-5-phenylpentanenitrile
-
-
88.9% (2R)-2-hydroxy-5-phenylpentanenitrile and 11.1% (2S)-2-hydroxy-5-phenylpentanenitrile
-
?
cyanide + 5-hydroxypentanal
(R)-2,6-dihydroxyhexanenitrile
-
by varying the different reaction parameters it is possible to reduce the extension of the undesirable non-enzymatic competing reaction and optimize the optical purity of the cyanohydrin product. Best results are obtained at 15°C
-
-
?
cyanide + acetophenone
(2R)-hydroxyphenylpropionitrile
-
(R)-cyanohydrin is formed with 1% yield and 99% enantiomeric excess, after 96 h at pH 4.0 and 5°C, cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase
-
-
r
cyanide + furan-2-carbaldehyde
(2R)-(furan-2-yl)(hydroxy)acetonitrile
-
isoenzyme HNL5
-
-
?
cyanide + naphthalen-2-ylacetaldehyde
(2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
-
-
3.5% (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile and 96.5% (2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
-
?
cyanide + naphthalen-2-ylacetaldehyde
(2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile + (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
-
-
33.2% (2R)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile and 66.8% (2S)-2-hydroxy-3-(naphthalen-2-yl)propanenitrile
-
?
cyanide + naphthalene-1-carbaldehyde
(2R)-hydroxy(naphthalen-1-yl)acetonitrile
-
isoenzyme HNL5
-
-
?
cyanide + naphthalene-2-carbaldehyde
(2R)-hydroxy(naphthalen-2-yl)acetonitrile
-
isoenzyme HNL5
-
-
?
cyanide + naphthalene-2-carbaldehyde
(2R)-hydroxy(naphthalen-2-yl)ethanenitrile
-
-
97.6% (2R)-hydroxy(naphthalen-2-yl)ethanenitrile and 2.4% (2S)-hydroxy(naphthalen-2-yl)ethanenitrile
-
?
cyanide + pyridine-3-carbaldehyde
(2R)-hydroxy(pyridin-3-yl)acetonitrile
-
isoenzyme HNL5
-
-
?
cyanide + tetrahydro-2H-pyran-2-carbaldehyde
(2S)-hydroxy-[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile + (2R)-hydroxy-[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile + (2S)-hydroxy-[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile + (2R)-hydroxy-[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydro-2H-pyran-2-carbaldehyde is converted to 47.6% (2S)-hydroxy[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 4.6% (2R)-hydroxy[(2R)-tetrahydro-2H-pyran-2-yl]ethanenitrile, 42.6% (2S)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile and 5.2% (2R)-hydroxy[(2S)-tetrahydro-2H-pyran-2-yl]ethanenitrile
-
?
cyanide + tetrahydrofuran-2-carbaldehyde
(2S)-hydroxy-[(2R)-tetrahydrofuran-2-yl]ethanenitrile + (2R)-hydroxy-[(2R)-tetrahydrofuran-2-yl]ethanenitrile + (2S)-hydroxy-[(2S)-tetrahydrofuran-2-yl]ethanenitrile + (2R)-hydroxy-[(2S)-tetrahydrofuran-2-yl]ethanenitrile
-
-
the natural substrate benzaldehyde is stereoselectively converted to (R)-mandelonitrile. The non-natural substrate tetrahydrofuran-2-carbaldehyde is converted to 33.7% (2S)-hydroxy[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 16.2% (2R)-hydroxy[(2R)-tetrahydrofuran-2-yl]ethanenitrile, 35.6% (2S)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile and 14.5% (2R)-hydroxy[(2S)-tetrahydrofuran-2-yl]ethanenitrile
-
?
cyanide + thiophene-2-carbaldehyde
(2R)-hydroxy(thiophen-2-yl)acetonitrile
-
isoenzyme HNL5
-
-
?
HCN + 2-allylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-allylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-allylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-allylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-allyloxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-allyloxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-allyloxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-allyloxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-ethoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-ethoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-ethoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-ethoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-ethylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-ethylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-ethylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-methylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-methoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-methoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-methoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-methoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-methylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-methylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-methylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-methylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-n-propoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-n-propoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-n-propoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-n-propoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-n-propylcyclohexanone
cis-(1R,2S)-1-hydroxy-2-n-propylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 2-n-propylcyclohexanone
trans-(1R,2R)-1-hydroxy-2-n-propylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 3-methoxycyclohexanone
cis-(1R,3S)-1-hydroxy-3-methoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 3-methoxycyclohexanone
trans-(1R,3R)-1-hydroxy-3-methoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + 3-methylcyclohexanone
cis-(1R,3S)-1-hydroxy-3-methylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 3-methylcyclohexanone
trans-(1R,3R)-1-hydroxy-3-methylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 3-trifluoromethylcyclohexanone
cis-(1R,3S)-1-hydroxy-3-trifluoromethylcyclohexanecarbonitrile
-
-
-
-
?
HCN + 3-trifluoromethylcyclohexanone
trans-(1R,3R)-1-hydroxy-3-trifluoromethylcyclohexanecarbonitrile
-
-
-
-
?
HCN + benzaldehyde
(R)-mandelonitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
HCN + decanal
(R)-2-hydroxyundecanenitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
HCN + dodecanal
(R)-2-hydroxytridecanenitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
HCN + iso-propoxycyclohexanone
cis-(1S,2S)-1-hydroxy-2-iso-propoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + iso-propoxycyclohexanone
trans-(1S,2R)-1-hydroxy-2-iso-propoxycyclohexanecarbonitrile
-
-
-
-
?
HCN + undecanal
(R)-2-hydroxydodecanenitrile
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remains good
-
-
?
additional information
?
-
-
naphthyl and alkoxy substituents in the alpha- and also in the beta-position to the aldehyde group significantly influence the stereochemical outcome of the oxynitrilase-catalyzed transformation. No activity with methoxy(phenyl)acetaldehyde
-
-
?
(R)-mandelonitrile
cyanide + benzaldehyde
in a large number of plant species hydroxynitrile lyases catalyzes the decomposition of cyanohydrins in order to generate hydrogen cyanide upon tissue damage. Hydrogen cyanide serves as a deterrent against herbivores and fungi
-
-
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
99% yield, 99% enantiomeric excess
-
?
cyanide + benzaldehyde
(R)-mandelonitrile
the formation of (R)-mandelonitrile from benzaldehyde and cyanide catalyzed by Prunus amygdalus hydroxynitrile lyase is chosen as a model reaction for the development and validation of a process model for production of (R)-cyanohydrins in an aqueous-organic biphasic-stirred tank reactor with an unknown interfacial area operated in batch mode. At 5°C and pH 5.5 the nonenzymatic reaction towards rac-mandelonitrile is largely suppressed
-
-
r
(R)-mandelonitrile
cyanide + benzaldehyde
-
modeling studies provide insights into the mechanism of cyanogenesis
-
-
r
cyanide + 2-chlorobenzaldehyde
(R)-2-chloromandelonitrile
-
synthesis of (R)-2-chloromandelonitrile with a yield of 100% and an enantiomeric excess of 21%
-
-
?
cyanide + 4-fluorobenzaldehyde
(R)-4-fluoromandelonitrile
-
synthesis of (R)-4-fluoromandelonitrile with a yield of 100% and an enantiomeric excess value of 72%
-
-
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
-
90.3% yield and 100% enantiomeric excess after 2 h
-
?
cyanide + benzaldehyde
(R)-mandelonitrile
-
cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase achieve the synthesis of (R)-mandelonitrile, (R)-cyanohydrin is formed with 93% yield and 99% enantiopurity
-
-
r
cyanide + benzaldehyde
(R)-mandelonitrile
-
synthesis of (R)-mandelonitrile with a yield of 100% and an enantiomeric excess of 99%
-
-
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
-
-
96.3% (2R)-2-hydroxy-3-phenylpropanenitrile and 3.7% (2S)-2-hydroxy-3-phenylpropanenitrile
-
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
-
isoenzyme HNL5
-
-
?
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
(R)-mandelonitrile
cyanide + benzaldehyde
in a large number of plant species hydroxynitrile lyases catalyzes the decomposition of cyanohydrins in order to generate hydrogen cyanide upon tissue damage. Hydrogen cyanide serves as a deterrent against herbivores and fungi
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
absolute requirement of oxidized FAD as cofactor. Enzyme activity requires the FAD cofactor to be bound in its oxidized form. The observed inactivation upon cofactor reduction is largely caused by the reversal of the electrostatic potential within the active site
FAD
FAD-dependent enzyme, the FAD cofactor is deeply buried within the molecule and is completely isolated from bulk solvent
FAD
there is no evidence that the flavin cofactor directly participates in the reaction
FAD
benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized
FAD
thee structure of PaHNL5 in complex with benzyl alcohol shows that this compound binds too far away from the FAD cofactor in order to directly participate in the redox mechanism proposed for aryl-alcohol oxidases
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
reaction in a two phase solvent system aqueous buffer and ionic liquid. When compared to the use of organic solvents as the nonaqueous phase, the reaction rate is significantly increased whereas the enantioselectivity remained good
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
estimation of kinetic parameters by progress curve analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
estimation of kinetic parameters by progress curve analysis
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
-
at low pH very low amounts of crude enzyme catalyse stereoselective hydroxypivalaldehyde cyanohydrin formation in water based reaction systems
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
temporal and spatial expression patterns in flowers and mature seeds. Highest expression levels are detected during floral development. High level of expression in parenchymal cells, both in petals and in the style of the carpe
temporal and spatial expression patterns in flowers and mature seeds
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in a process called cyanogenesis. They possess an important biological role in plant defense against herbivoral and fungal attack due to the bitter taste and the release of toxic hydrogen cyanide upon tissue disruption
physiological function
the enzyme is involved in aprocess called cyanogenesis. They possess an important biological role in plant defense against herbivoral and fungal attack due to the bitter taste and the release of toxic hydrogen cyanide upon tissue disruption
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). MDL1_PRUDU
559
0
61100
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
the mass difference between the glycosylated and deglycosylated form of the recombinant protein expressed in Aspergillus niger averages to 25 kDa, which indicates that more than one sugar unit is attached to the glycosylated Asn residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3D structural data of the enzyme with the reaction product benzaldehyde bound within the active site, which allow unambiguous assignment of the location of substrate binding
crystal structuture of mutant V317A of hydroxynitrile lyase isoenzyme 5 in complex with benzyl alcohol. The structure of is determined at a resolutionof 2.3 A by molecular replacement
triclinic crystals grown in hanging drops, 1.5 A resolution, space group P1 with cell parameters a = 56.2 A, b = 67.5 A, c = 79.8
vapor diffusion method, high resolution X-ray structure of the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) expressed in Aspergillus niger and its complex with benzyl alcohol. In PaHNLs benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized
hanging drop vapor diffusion using polyethylene glycol 4000 and isopropanol as coprecipitants. The crystals belong to the monoclinic space group P2(1) with unit cell parameters a = 69.9, b = 95.1, c = 95.6 A, and beta = 118.5 degrees. A complete set of diffraction data collected to 2.6 A resolution on native crystals of isoenzyme III
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I108M/A111G
-
mutant with improved catalytic properties: recovery of a 89.9% yield of (R)-2-chloromandelonitrile with an enantiomeric excess of 97.6% enantiomeric excess, about 4% residual aldehyde. The mutant also contains two silent mutations at position 85 and position 432
L1Q/A111G
-
activity is similar to wild-type enzyme with its preferred substrate benzaldehyde. Directed evolution of PaHNL5/L1Q/A11G
L1Q/N3I/I108M/A111G
-
mutant with improved catalytic properties: recovery of a 92.7% yield of (R)-2-chloromandelonitrile with an ee of 98.6% enantiomeric excess, about 2% residual aldehyde, the mutant also contains two silent mutations at position 85 and position 432
additional information
-
directed evolution of PaHNL5/L1Q/A11G (a mutant with activity is similar to wild-type enzyme with its preferred substrate benzaldehyde). 10000 transformants are screened for cleavage or synthesis of (R)-2-chloromandelonitrile
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
70
76
65
in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3
70
in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3
76
in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable
-
the cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase can be reused several times without loss of enantioselectivity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partly, as crosslinked enzyme aggregates. Optimal conditions are initial glutaraldehyde concentration of 25% w/v, ammonium sulfate saturation concentration of 43% w/v, and crosslinking time of 18 h
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant V317A of hydroxynitrile lyase isoenzyme 5 is expressed in Aspergillus niger
the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) is expressed in Aspergillus niger. The recombinant protein is highly glycosylated as confirmed by SDS-page and mass spectrometry
heterologously expression of the His-tagged hydroxynitrile lyase isoenzymes (HNL1, HNL2, HNL4 and HNL5) in Pichia pastoris
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
synthesis
development and validation of a process model for production of (R)-cyanohydrins in an aqueous-organic biphasic-stirred tank reactor with an unknown interfacial area operated in batch mode. The formation of (R)-mandelonitrile from benzaldehyde and cyanide catalyzed by Prunus amygdalus hydroxynitrile lyase is chosen as a model reaction. Methyl tert-butyl ether is selected as the organic solvent and the reaction conditions are 5°C and pH 5.5 at which the nonenzymatic reaction towards rac-mandelonitrile is largely suppressed
synthesis
hydroxynitrile lyases are proficient biocatalysts for the stereospecific synthesis of cyanohydrins
synthesis
-
(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable. Application in microaqueous medium, superior biocatalyst for the enantioselective hydrocyanation of slow-reacting aldehydes
synthesis
-
production of (R)-hydroxypivalaldehyde cyanohydrin, the chiral key precursor in hydroxynitrile lyase based (R)-pantlactone synthesis
synthesis
-
purification of enzyme as crosslinked enzyme aggregates and application for synthesis of enantiopure cyanohydrins
synthesis
-
the enzyme is a powerful and cheap biocatalyst in the synthesis of (R)-mandelonitrile and may be used in combination with nitrilases to produce enantiopure mandelic acids
synthesis
-
the immobilization of partially purified hydroxynitrile lyase from Prunus dulcis as crosslinked enzyme aggregate is a very promising tool owing to its ease of preparation, cheapness, and efficiency in the preparation of enantiopure cyanohydrins. Response surface methodology provides an effective way for the optimization of the preparation of PdHNL-crosslinked enzyme aggregate. The synthesis of (R)-mandelonitrile, (R)-2-chloromandelonitrile, (R)-3,4-dihydroxymandelonitrile, (R)-2-hydroxy-4-phenyl butyronitrile, (R)-4-bromomandelonitrile, (R)-4-fluoromandelonitrile, and (R)-4-nitromandelonitrile is achieved with high yield and enantiomeric excess
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wajant, H.; Foerster, S.; Selmar, D.; Effenberger, F.; Pfizenmaier, K.
Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum
Plant Physiol.
109
1231-1238
1995
Phlebodium aureum, Prunus dulcis (O24243)
Lauble, H.; Mueller, K.; Schindellin, H.; Foerster, S.; Effenberger, F.
Crystallization and preliminary X-ray diffraction studies of mandelonitrile lyase from almonds
Proteins Struct. Funct. Genet.
19
343-347
1994
Prunus dulcis
Willeman, W.F.; Hanefeld, U.; Straathof, A.J.J.; Heijnen, J.J.
Estimation of kinetic parameters by progress curve analysis for the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase
Enzyme Microb. Technol.
27
423-433
2000
Prunus dulcis
de Gonzalo, G.; Brieva, R.; Gotor, V.
(R)-Oxynitrilase-catalyzed transformation of omega-hydroxyalkanals
J. Mol. Catal. B
19-20
223-230
2002
Prunus dulcis
-
Dreveny, I.; Kratky, C.; Gruber, K.
The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesis
Protein Sci.
11
292-300
2002
Prunus dulcis
Dreveny, I.; Gruber, K.; Glieder, A.; Thompson, A.; Kratky, C.
The hydroxynitrile L-lyase from almond: A lyase that looks like an oxidoreductase
Structure
9
803-815
2001
Prunus dulcis (O24243), Prunus dulcis
Bianchi, P.; Roda, G.; Riva, S.; Danieli, B.; Zabelinskaja-Mackova, A.; Griengl, H.
On the selectivity of oxynitrilases towards alpha-oxygenated aldehydes
Tetrahedron
57
2213-2220
2001
Prunus dulcis
-
Weis, R.; Poechlauer, P.; Bona, R.; Skranc, W.; Luiten, R.; Wubbolts, M.; Schwab, H.; Glieder, A.
Biocatalytic conversion of unnatural substrates by recombinant almond R-HNL isoenzyme 5
J. Mol. Catal. B
29
211-218
2004
Prunus dulcis
-
van Langen, L.M.; Selassa, R.P.; van Rantwijk, F.; Sheldon, R.A.
Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation
Org. Lett.
7
327-329
2005
Prunus dulcis
Gaisberger, R.P.; Fechter, M.H.; Griengl, H.
The first hydroxynitrile lyase catalysed cyanohydrin formation in ionic liquids
Tetrahedron
15
2959-2963
2004
Prunus dulcis
-
Kobler, C.; Bohrer, A.; Effenberger, F.
Hydroxynitrile lyase-catalyzed addition of HCN to 2- and 3-substituted cyclohexanones
Tetrahedron
60
10397-10410
2004
Prunus dulcis
-
Liu, Z.; Pscheidt, B.; Avi, M.; Gaisberger, R.; Hartner, F.S.; Schuster, C.; Skranc, W.; Gruber, K.; Glieder, A.
Laboratory evolved biocatalysts for stereoselective syntheses of substituted benzaldehyde cyanohydrins
Chembiochem
9
58-61
2008
Prunus dulcis
Pscheidt, B.; Avi, M.; Gaisberger, R.; Hartner, F.S.; Skranc, W.; Glieder, A.
Screening hydroxynitrile lyases for (R)-pantolactone synthesis
J. Mol. Catal. B
52-53
183-188
2008
Prunus dulcis
-
Dreveny, I.; Andryushkova, A.S.; Glieder, A.; Gruber, K.; Kratky, C.
Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity
Biochemistry
48
3370-3377
2009
Prunus dulcis (O24243)
Willeman, W.F.; Gerrits, P.J.; Hanefeld, U.; Brussee, J.; Straathof, A.J.; van der Gen, A.; Heijnen, J.J.
Development of a process model to describe the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase in an aqueous-organic biphasic reactor
Biotechnol. Bioeng.
77
239-247
2002
Prunus dulcis (O24243)
Fechter, M.H.; Gruber, K.; Avi, M.; Skranc, W.; Schuster, C.; Pchlauer, P.; Klepp, K.O.; Griengl, H.
Stereoselective biocatalytic synthesis of (S)-2-hydroxy-2-methylbutyric acid via substrate engineering by using "thio-disguised" precursors and oxynitrilase catalysis
Chemistry
13
3369-3376
2007
Prunus dulcis
Suelves, M.; Puigdomenech, P.
Molecular cloning of the cDNA coding for the (R)-(+)-mandelonitrile lyase of Prunus amygdalus: temporal and spatial expression patterns in flowers and mature seeds
Planta
206
388-393
1998
Prunus dulcis (O24243), Prunus dulcis
Roda, G.; Riva, S.; Danieli, B.
Almond oxynitrilase-catalyzed transformation of aldehydes is strongly influenced by naphthyl and alkoxy substituents
Tetrahedron
10
3939-3949
1999
Prunus dulcis
-
Yildirim, D.; Tuekel, S.S.; Alagoez, D.
Crosslinked enzyme aggregates of hydroxynitrile lyase partially purified from Prunus dulcis seeds and its application for the synthesis of enantiopure cyanohydrins
Biotechnol. Prog.
30
818-827
2014
Prunus dulcis
Zheng, Y.; Xu, J.; Wang, H.; Lin, G.; Hong, R.; Yu, H.
Hydroxynitrile lyase isozymes from Prunus communis identification, characterization and synthetic applications
Adv. Synth. Catal.
359
1185-1193
2017
Prunus dulcis
-
Alagoez, D.; Tuekel, S.S.; Yildirim, D.
Enantioselective synthesis of various cyanohydrins using covalently immobilized preparations of hydroxynitrile lyase from Prunus dulcis
Appl. Biochem. Biotechnol.
177
1348-1363
2015
Prunus dulcis
Yildirim, D.; Tkel, S.S.; Alagz, D.
Crosslinked enzyme aggregates of hydroxynitrile lyase partially purified from Prunus dulcis seeds and its application for the synthesis of enantiopure cyanohydrins
Biotechnol. Prog.
30
818-827
2014
Prunus dulcis
Pavkov-Keller, T.; Bakhuis, J.; Steinkellner, G.; Jolink, F.; Keijmel, E.; Birner-Gruenberger, R.; Gruber, K.
Structures of almond hydroxynitrile lyase isoenzyme 5 provide a rationale for the lack of oxidoreductase activity in flavin dependent HNLs
J. Biotechnol.
235
24-31
2016
Prunus dulcis (O24243), Prunus dulcis
EXTERNAL LINKS (specific for EC-Number 4.1.2.10)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
