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Literature summary for 4.1.2.47 extracted from

  • Kawahara, N.; Asano, Y.
    Mutagenesis of an Asn156 residue in a surface region of S-selective hydroxynitrile lyase from Baliospermum montanum enhances catalytic efficiency and enantioselectivity (2015), ChemBioChem, 16, 1891-1895 .
    View publication on PubMed
Search for more literature for 4.1.2.47

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-zyüe and mutant enzymes in Escherichia coli Baliospermum montanum

Protein Variants

Protein Variants Comment Organism
H103C the mutated enzyme shows low enantioselectivity and specific activity for (S)-mandelonitrile synthesis. (S)-Mandelonitrile enantiomeric excess is 60% Baliospermum montanum
H103C/N156D hydroxynitrile lyase of mutant enzyme H103C/N156D is approximately four times higher than that for mutant enzyme H103C. (S)-Mandelonitrile enantiomeric excess is 32% Baliospermum montanum
H103C/N156G the specific activity of the H103C/N156G mutant for (S)-mandelonitrile production is raised to 154 U/mg (wild-type hydroxynitrile lyase: 52 U/mg). The enantiomeric excess is increased to 93% (wild-type: 55%). Km-value for (R)-mandelonitrile and kcat for (S)-mandelonitrile increase by the mutation at Asn156, thus contributing to the increase in enantiomeric excess Baliospermum montanum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.28
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C Baliospermum montanum
0.34
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C Baliospermum montanum
0.47
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156D Baliospermum montanum
0.49
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156G Baliospermum montanum
0.61
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156D Baliospermum montanum
1.49
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156G Baliospermum montanum

Organism

Organism UniProt Comment Textmining
Baliospermum montanum D1MX73
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Baliospermum montanum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-mandelonitrile low activity Baliospermum montanum cyanide + benzaldehyde
-
 r
(S)-mandelonitrile
-
 Baliospermum montanum cyanide + benzaldehyde
-
 r
cyanide + benzaldehyde
-
 Baliospermum montanum (S)-mandelonitrile
-
 r

Synonyms

Synonyms Comment Organism
S-selective hydroxynitrile lyase
-
 Baliospermum montanum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.98
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C Baliospermum montanum
9.27
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156D Baliospermum montanum
12.7
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156G Baliospermum montanum
52.9
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C Baliospermum montanum
88.1
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156D Baliospermum montanum
122
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156G Baliospermum montanum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
8.81
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156G Baliospermum montanum
15.4
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156D Baliospermum montanum
29.1
-
 (R)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C Baliospermum montanum
157
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C Baliospermum montanum
191
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156D Baliospermum montanum
251
-
 (S)-mandelonitrile pH 4.23, 25°C, mutant enzyme H103C/N156G Baliospermum montanum