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Literature summary for 4.1.2.10 extracted from

  • 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 (2013), Appl. Environ. Microbiol., 79, 4727-4733.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.2.10

Application

Application Comment Organism
synthesis fusion of enzyme to different fluorescent reporter proteins. Flavin-based fluorescent reporter fusions convert 95% benzaldehyde to (R)-mandelonitrile within 60 min at pH 4.75, with 96% enantiomeric excess Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
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 Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9LFT6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
HCN + 2-chlorobenzaldehyde
-
 Arabidopsis thaliana (R)-2-hydroxy-2-(2-chlorophenyl)acetonitrile
-
 ?
HCN + benzaldehyde
-
 Arabidopsis thaliana (R)-2-hydroxy-2-phenylacetonitrile
-
 ?

Synonyms

Synonyms Comment Organism
HNL
-
 Arabidopsis thaliana

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.75
-
 wild-type, half-life 2.2 min, flavin-based fluorescent reporter fusion protein half-life 55-95 min Arabidopsis thaliana