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Information on EC 4.1.2.10 - (R)-mandelonitrile lyase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LFT6

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     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.10 (R)-mandelonitrile lyase
IUBMB 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).
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9LFT6
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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, ejhnl, acix9_0562, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R-selective HNL
-
R-selective hydroxynitrile lyase
-
(R)-(+)-Mandelonitrile lyase
-
-
-
-
(R)-Mandelonitrile lyase
-
-
-
-
(R)-Oxynitrilase
-
-
-
-
D-alpha-hydroxynitrile lyase
-
-
-
-
D-Hydroxynitrile lyase
-
-
-
-
D-Oxynitrilase
-
-
-
-
Hydroxynitrile lyase
-
-
-
-
Lyase, mandelonitrile
-
-
-
-
MDL
-
-
-
-
Oxynitrilase
-
-
-
-
PhaMDL
-
-
-
-
R-hydroxynitrile lyase
-
-
R-selective hydroxynitrile lyase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyanohydrin formation
-
-
-
-
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 hide
9024-43-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-mandelonitrile
cyanide + benzaldehyde
show the reaction diagram
-
-
-
?
cyanide + (2E)-hex-2-enal
(3E)-2-hydroxyhept-3-enenitrile
show the reaction diagram
-
53% enantiomeric excess
-
?
cyanide + 2-bromobenzaldehyde
(2R)-(2-bromophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
98% enantiomeric excess
-
?
cyanide + 2-chlorobenzaldehyde
(2R)-(2-chlorophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
99% enantiomeric excess
-
?
cyanide + 2-fluorobenzaldehyde
(2R)-(2-fluorophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
99% enantiomeric excess
-
?
cyanide + 2-iodobenzaldehyde
(2R)-(2-iodophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
more than 95% enantiomeric excess
-
?
cyanide + 3-bromobenzaldehyde
(2R)-(3-bromophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
95% enantiomeric excess
-
?
cyanide + 3-chlorobenzaldehyde
(2R)-(3-chlorophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
more than 99% enantiomeric excess
-
?
cyanide + 3-fluorobenzaldehyde
(2R)-(3-fluorophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
more than 99% enantiomeric excess
-
?
cyanide + 3-iodobenzaldehyde
(2R)-(3-iodophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
93% enantiomeric excess
-
?
cyanide + 3-phenoxybenzaldehyde
(2R)-2-hydroxy-2-(3-phenoxyphenyl)acetonitrile
show the reaction diagram
-
more than 95% enantiomeric excess
-
?
cyanide + 3-phenylpropanal
(2R)-2-hydroxy-4-phenylbutanenitrile
show the reaction diagram
-
68% enantiomeric excess
-
?
cyanide + 4-bromobenzaldehyde
(2R)-(4-bromophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
more than 99% enantiomeric excess
-
?
cyanide + 4-chlorobenzaldehyde
(2R)-(4-chlorophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
more than 99% enantiomeric excess
-
?
cyanide + 4-fluorobenzaldehyde
(2R)-(4-fluorophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
more than 99% enantiomeric excess
-
?
cyanide + 4-hydroxybenzaldehyde
(2R)-(4-hydroxyphenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
97% enantiomeric excess
-
?
cyanide + 4-iodobenzaldehyde
(2R)-(4-iodophenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
92% enantiomeric excess
-
?
cyanide + 4-methoxybenzaldehyde
(2R)-(4-methoxyphenyl)(hydroxy)ethanenitrile
show the reaction diagram
-
68% enantiomeric excess
-
?
cyanide + 6-methylhept-5-en-2-one
(2R)-2-hydroxy-2,6-dimethylhept-5-enenitrile
show the reaction diagram
-
-
-
?
cyanide + benzaldehyde
(R)-mandelonitrile
show the reaction diagram
-
more than 99% enantiomeric excess
-
?
cyanide + cyclohexanone
1-hydroxycyclohexanecarbonitrile
show the reaction diagram
-
-
-
?
cyanide + decanal
(2R)-2-hydroxyundecanal
show the reaction diagram
-
56% enantiomeric excess
-
?
cyanide + hexan-2-one
(2R)-2-hydroxy-2-methylhexanenitrile
show the reaction diagram
-
95% enantiomeric excess
-
?
cyanide + hexanal
(2R)-2-hydroxyheptanenitrile
show the reaction diagram
-
98% enantiomeric excess
-
?
cyanide + phenylacetaldehyde
(2R)-2-hydroxy-3-phenylpropanenitrile
show the reaction diagram
-
96% enantiomeric excess
-
?
cyanide + thiophene-2-carbaldehyde
hydroxy(thiophen-2-yl)ethanenitrile
show the reaction diagram
-
separation of enantiomers not posible
-
?
HCN + 2-chlorobenzaldehyde
(R)-2-hydroxy-2-(2-chlorophenyl)acetonitrile
show the reaction diagram
-
-
-
?
HCN + benzaldehyde
(R)-2-hydroxy-2-phenylacetonitrile
show the reaction diagram
-
-
-
?
nitromethane + 2-chlorobenzaldehyde
(1R)-1-(2-chlorophenyl)-2-nitroethanol
show the reaction diagram
-
34% yield, 68% enantiomeric excess
-
?
nitromethane + 3-methoxybenzaldehyde
(1R)-1-(3-methoxyphenyl)-2-nitroethanol
show the reaction diagram
-
17% yield, 91% enantiomeric excess
-
?
nitromethane + 4-fluorobenzaldehyde
(1R)-1-(4-fluorophenyl)-2-nitroethanol
show the reaction diagram
-
20% yield, 81% enantiomeric excess
-
?
nitromethane + benzaldehyde
(1R)-2-nitro-1-phenylethanol
show the reaction diagram
30% yield, 91% enantiomeric excess
-
-
?
(R)-4-hydroxymandelonitrile
cyanide + 4-hydroxybenzaldehyde
show the reaction diagram
-
-
-
-
r
(R)-mandelonitrile
cyanide + benzaldehyde
show the reaction diagram
2-chlorobenzaldehyde + nitromethane
1-(2-chlorophenyl)-2-nitroethanol
show the reaction diagram
-
34% yield after 2 h
-
?
2-methoxybenzaldehyde + nitromethane
1-(2-methoxyphenyl)-2-nitroethanol
show the reaction diagram
-
13% yield after 2 h
-
?
2-methylbenzaldehyde + nitromethane
1-(2-methylphenyl)-2-nitroethanol
show the reaction diagram
-
12% yield after 2 h
-
?
3-(2-naphthyl)benzaldehyde + nitromethane
(1R)-1-[3-(naphthalen-2-yl)phenyl]-2-nitroethanol
show the reaction diagram
-
7% yield after 2 h
-
?
3-chlorobenzaldehyde + nitromethane
1-(3-chlorophenyl)-2-nitroethanol
show the reaction diagram
-
17% yield after 2 h
-
?
3-methoxybenzaldehyde + nitromethane
1-(3-methoxyphenyl)-2-nitroethanol
show the reaction diagram
-
17% yield after 2 h
-
?
3-methylbenzaldehyde + nitromethane
1-(3-methylphenyl)-2-nitroethanol
show the reaction diagram
-
12% yield after 2 h
-
?
4-bromobenzaldehyde + nitromethane
1-(4-bromophenyl)-2-nitroethanol
show the reaction diagram
-
20% yield after 2 h
-
?
4-chlorobenzaldehyde + nitromethane
1-(4-chlorophenyl)-2-nitroethanol
show the reaction diagram
-
9% yield after 2 h
-
?
4-fluorobenzaldehyde + nitromethane
1-(4-fluorophenyl)-2-nitroethanol
show the reaction diagram
-
9% yield after 2 h
-
?
4-methoxybenzaldehyde + nitromethane
1-(4-methoxyphenyl)-2-nitroethanol
show the reaction diagram
-
2% yield after 2 h
-
?
4-methylbenzaldehyde + nitromethane
1-(4-methylphenyl)-2-nitroethanol
show the reaction diagram
-
11% yield after 2 h
-
?
benzaldehyde + nitromethane
(R)-2-nitro-1-phenylethanol
show the reaction diagram
-
30% yield after 2 h
-
?
cyanide + 4-hydroxybenzaldehyde
(R)-4-hydroxymandelonitrile
show the reaction diagram
-
-
-
-
r
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no inhibition by acetate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
(R)-4-hydroxymandelonitrile
-
pH 5.0, 25°C
6
4-hydroxybenzaldehyde
-
pH 5.0, 25°C
6
benzaldehyde
-
pH 6.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.2
wild-type, 25°C, pH 4.75
133.6
wild-type, 25°C, pH 6.0
227
surface-modified mutant, 25°C, pH 5.75
23.6
surface-modified mutant, 25°C, pH 4.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.25
1.4 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme, immobilized on cellulosic carrier materials Avicel)
4.5
pH-dependent half-lives: 1.5 min (wild-type enzyme), 1.5 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme), 2.1 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme, immobilized on cellulosic carrier materials Avicel)
4.75
pH-dependent half-lives: 4.4 min (wild-type enzyme), 5.5 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme), 30.6 min (family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi fused to a fluorescent reporter module and the Arabidopsis thaliana hydroxynitrile lyase as target enzyme, immobilized on cellulosic carrier materials Avicel)
5.75
surface-modified mutant
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
surface-modified mutant, less than 10% of maximum activity
4.75
wild-type, less than 10% of maximum activity
5
-
almost inactive below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
isoelectric focusing, wild-type
5.3
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HNL_ARATH
258
0
29217
Swiss-Prot
Mitochondrion (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
the enzyme forms dimers in solution
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure at a crystallographic resolution of 2.5 A and comparison with the S-selective HNL from Hevea brasiliensis. The structures exhibit an alpha/beta-hydrolase fold and a Ser-His-Asp catalytic triad. Modeling of complexes of the enzymes with both (R)- and (S)-mandelonitrile leads to a catalytic mechanism, in which His236 from the catalytic triad acts as a general base and the emerging negative charge on the cyano group is stabilized by main-chain amide groups and an alpha-helix dipole very similar to alpha/beta-hydrolases
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208N
less than 2% residual activity
H236F
less than 2% residual activity
M237K
no residual activity
M237L
100% residual activity
N12T
less than 2% residual activity
N12T/M237K
expression results in insoluble protein
S81A
less than 2% residual activity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.75
wild-type, half-life 2.2 min, flavin-based fluorescent reporter fusion protein half-life 55-95 min
726741
5
20°C, wild-type, half-life 0.16 h, surface-modified mutant, half-life 2.23 h
727311
6
20°C, wild-type, half-life 60 h, surface-modified mutant, half-life 52.2 h
727311
5.4
-
half-life time: 2 h, the deactivation of the enzyme at slightly acidic pH is a result of pronounced structural unfolding
704762
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
pH 5.0, wild-type, half-life 18 min, surface-modified mutant, half-life 137 min
10
pH 5.0, wild-type, half-life 23.6 min, surface-modified mutant, half-life 136 min
20
pH 5.0, wild-type, half-life 9.6 min, surface-modified mutant, half-life 134 min
0 - 20
-
stable
10
-
half-life time: more than 96 h
20
-
half-life time: 80 h
30
-
half-life time: 33 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the fusion protein of Arabidopsis thaliana hydroxynitrile lyase and a family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi and a fluorescent reporter module protein shows increases stability at weakly acidic pH values, which is further increased by immobilization
the enzyme is stabilized by addition of sorbitol and saccharose
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
butyl acetate
synthesis of (R)-beta-nitro alcohols, highest enantioselectivity is obtained with n-butyl acetate as solvent with an optimum aqueous phase content of 50% (v/v)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the fused family 2 carbohydrate-binding module enables the purification and simultaneous immobilization of Arabidopsis thaliana hydroxynitrile lyase on various cellulosic carrier materials
ammonium sulfate precipitation and Ni Sepharose column chromatography
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana hydroxynitrile lyase fused to family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi and to a fluorescent reporter module
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Andexer, J.; von Langermann, J.; Mell, A.; Bocola, M.; Kragl, U.; Eggert, T.; Pohl, M.
An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an alpha/beta-hydrolase fold
Angew. Chem. Int. Ed. Engl.
46
8679-8681
2007
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
Manually annotated by BRENDA team
Guterl, J.K.
Andexer, J.N.; Sehl, T.; von Langermann, J.; Frindi-Wosch, I.; Rosenkranz, T.; Fitter, J.; Gruber, K.; Kragl, U.; Eggert, T.; Pohl, M.: Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases with alpha/beta-hydrolase fold
J. Biotechnol.
141
166-173
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Fuhshuku, K.; Asano, Y.
Synthesis of (R)-beta-nitro alcohols catalyzed by R-selective hydroxynitrile lyase from Arabidopsis thaliana in the aqueous-organic biphasic system
J. Biotechnol.
153
153-159
2011
Arabidopsis thaliana, Arabidopsis thaliana (Q9LFT6)
Manually annotated by BRENDA team
Scholz, K.E.; Kopka, B.; Wirtz, A.; Pohl, M.; Jaeger, K.E.; Krauss, U.
Fusion of a flavin-based fluorescent protein to hydroxynitrile lyase from Arabidopsis thaliana improves enzyme stability
Appl. Environ. Microbiol.
79
4727-4733
2013
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
Manually annotated by BRENDA team
Andexer, J.N.; Staunig, N.; Eggert, T.; Kratky, C.; Pohl, M.; Gruber, K.
Hydroxynitrile lyases with alpha/beta-hydrolase fold: two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms
ChemBioChem
13
1932-1939
2012
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
Manually annotated by BRENDA team
Okrob, D.; Metzner, J.; Wiechert, W.; Gruber, K.; Pohl, M.
Tailoring a stabilized variant of hydroxynitrile lyase from Arabidopsis thaliana
ChemBioChem
13
797-802
2012
Arabidopsis thaliana (Q9LFT6), Arabidopsis thaliana
Manually annotated by BRENDA team
Kopka, B.; Diener, M.; Wirtz, A.; Pohl, M.; Jaeger, K.E.; Krauss, U.
Purification and simultaneous immobilization of Arabidopsis thaliana hydroxynitrile lyase using a family 2 carbohydrate-binding module
Biotechnol. J.
10
811-819
2015
Arabidopsis thaliana (Q9LFT6)
Manually annotated by BRENDA team