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Literature summary for 4.1.2.47 extracted from

  • Padhi, S.K.; Fujii, R.; Legatt, G.A.; Fossum, S.L.; Berchtold, R.; Kazlauskas, R.J.
    Switching from an esterase to a hydroxynitrile lyase mechanism requires only two amino acid substitutions (2010), Chem. Biol., 17, 863-871.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
(S)-mandelonitrile in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication Hevea brasiliensis
1.4
-
(S)-mandelonitrile in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication Manihot esculenta

Organism

Organism UniProt Comment Textmining
Hevea brasiliensis
-
-
-
Manihot esculenta
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-mandelonitrile
-
Hevea brasiliensis cyanide + benzaldehyde
-
?
(S)-mandelonitrile
-
Manihot esculenta cyanide + benzaldehyde
-
r
cyanide + benzaldehyde
-
Manihot esculenta (S)-mandelonitrile low enantioselectivity with 20% ee (S) r

Synonyms

Synonyms Comment Organism
(S)-selective hydroxynitrile lyase
-
Manihot esculenta
HNL
-
Hevea brasiliensis
HNL
-
Manihot esculenta

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.83
-
(S)-mandelonitrile in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication Hevea brasiliensis
21.67
-
(S)-mandelonitrile in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication Manihot esculenta

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.55
-
(S)-mandelonitrile in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication Hevea brasiliensis
15.83
-
(S)-mandelonitrile in 50 mM citrate buffer (pH 5.0), temperature not specified in the publication Manihot esculenta