4.1.2.10: (R)-mandelonitrile lyase
This is an abbreviated version!
For detailed information about (R)-mandelonitrile lyase, go to the full flat file.
Word Map on EC 4.1.2.10
-
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
- 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
Reaction
Synonyms
(R)-(+)-Mandelonitrile lyase, (R)-HNL, (R)-HNL5, (R)-hydroxynitrile lyase, (R)-Mandelonitrile lyase, (R)-Oxynitrilase, (R)-PeHNL, (R)-selective HNL, AciX9_0562, almond oxynitrilase, APHNL, AtHNL, cupin 2 conserved barrel domain protein, cupin 2 domain-containing protein, D-alpha-hydroxynitrile lyase, D-Hydroxynitrile lyase, D-Oxynitrilase, DtHNL1, EjHNL, FAD-HNL, HNL, HNL1, HNL2, HNL4, HNL5, Hydroxynitrile lyase, hydroynitrile lyase, Lyase, mandelonitrile, mandelonitrile lyase, MDL, Mdl1, NdHNL, Oxynitrilase, PaHNL, PaHNL1, PaHNL5, PaMDL, ParsHNL, PhaMDL, PmHNL, R-HNL, R-hydroxynitrile lyase, R-selective HNL, R-selective hydroxynitrile lyase
ECTree
4.1.2.10 (R)-mandelonitrile lyaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.1.2.10 - (R)-mandelonitrile lyase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N105Q
the mutant enzyme shows much lower thermostability, pH stability, and organic solvent tolerance than the hydroxynitrile lyase from leaves and that expressed in Pichia pastoris. kcat of the mutant enzyme is 1.3fold lower than the kcat of the wild-type enzyme, kcat/Km of the mutant enzyme is 2.3fold lower than the kcat/Km of the wild type enzyme from leaves
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
additional information
design of a surface-modified variant incorporating 11 changes in the amino acids on the protein surface to stabilze the protein at acidic pH. Mutant shows a broadened pH optimum towards the acidic range, along with enhancement of activity by up to twofold and significantly increased pH- and thermostabilities. The effect is probably due to a shift of the isoelectic point from pH 5.1 to 4.8. Mutant is applicable in aqueous/organic two-phase systems
additional information
-
design of a surface-modified variant incorporating 11 changes in the amino acids on the protein surface to stabilze the protein at acidic pH. Mutant shows a broadened pH optimum towards the acidic range, along with enhancement of activity by up to twofold and significantly increased pH- and thermostabilities. The effect is probably due to a shift of the isoelectic point from pH 5.1 to 4.8. Mutant is applicable in aqueous/organic two-phase systems
additional information
fusion of enzyme to different fluorescent reporter proteins. All fusion constructs retain enzymatic activity and fluorescence in vivo and in vitro, but show significant differences in activity and pH stability. Flavin-based fluorescent reporter fusions show almost 2 orders of magnitude-increased half-lives in the weakly acidic pH range compared to findings for the wild-type enzyme. This increased stability is apparently caused by oligomerization mediated via the flavin-based tag. The increased stability of the fusion proteins enables the efficient synthesis of (R)-mandelonitrile in an aqueous-organic two-phase system at a pH below 5
additional information
-
fusion of enzyme to different fluorescent reporter proteins. All fusion constructs retain enzymatic activity and fluorescence in vivo and in vitro, but show significant differences in activity and pH stability. Flavin-based fluorescent reporter fusions show almost 2 orders of magnitude-increased half-lives in the weakly acidic pH range compared to findings for the wild-type enzyme. This increased stability is apparently caused by oligomerization mediated via the flavin-based tag. The increased stability of the fusion proteins enables the efficient synthesis of (R)-mandelonitrile in an aqueous-organic two-phase system at a pH below 5
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
