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Literature summary extracted from

  • Li, H.; Zhu, S.; Zheng, G.
    Promiscuous (+)-gamma-lactamase activity of an amidase from nitrile hydratase pathway for efficient synthesis of carbocyclic nucleosides intermediate (2018), Bioorg. Med. Chem. Lett., 28, 1071-1076 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.2.B2 drug development the enzyme is an ideal catalyst for the preparation of carbocyclic nucleosides of pharmaceutical interest. IT can be used in a scalable bioprocess and is an efficient, economical, and environmentally route for producing optically pure (-)-gamma-lactam Rhodococcus erythropolis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.4 overexpression in Escherichia coli BL21(DE3) Rhodococcus erythropolis
3.5.2.B2 overexpression in Escherichia coli BL21(DE3) Rhodococcus erythropolis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.4 1.03
-
Benzamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 19
-
acetamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 24.1
-
Acrylamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 34.2
-
Propionamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.2.B2 53.9
-
2-azabicyclo[2.2.1]hept-5-en-3-one pH and temperature not specified in the publication Rhodococcus erythropolis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.4 Rhodococcus erythropolis
-
-
-
3.5.1.4 Rhodococcus erythropolis R4
-
-
-
3.5.2.B2 Rhodococcus erythropolis Q7DKE4
-
-
3.5.2.B2 Rhodococcus erythropolis R4 Q7DKE4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.4
-
Rhodococcus erythropolis
3.5.2.B2
-
Rhodococcus erythropolis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.4 acetamide + H2O
-
Rhodococcus erythropolis acetate + NH3
-
?
3.5.1.4 acetamide + H2O
-
Rhodococcus erythropolis R4 acetate + NH3
-
?
3.5.1.4 acrylamide + H2O
-
Rhodococcus erythropolis acrylate + NH3
-
?
3.5.1.4 acrylamide + H2O
-
Rhodococcus erythropolis R4 acrylate + NH3
-
?
3.5.1.4 benzamide + H2O
-
Rhodococcus erythropolis benzoate + NH3
-
?
3.5.1.4 benzamide + H2O
-
Rhodococcus erythropolis R4 benzoate + NH3
-
?
3.5.1.4 propionamide + H2O
-
Rhodococcus erythropolis propionate + NH3
-
?
3.5.1.4 propionamide + H2O
-
Rhodococcus erythropolis R4 propionate + NH3
-
?
3.5.2.B2 2-azabicyclo[2.2.1]hept-5-en-3-one + H2O i.e. Vince lactam. Promiscuous (+)-gamma-lactamase activity of a versatile amidase involved in the nitrile degradation pathway. The kcat for Vince lactam is higher than that of acetamide and acrylamide and lower than that of propionamide and benzamide, indicating that Vince lactam is a moderate preferable substrate Rhodococcus erythropolis (-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
?
3.5.2.B2 2-azabicyclo[2.2.1]hept-5-en-3-one + H2O i.e. Vince lactam. Promiscuous (+)-gamma-lactamase activity of a versatile amidase involved in the nitrile degradation pathway. The kcat for Vince lactam is higher than that of acetamide and acrylamide and lower than that of propionamide and benzamide, indicating that Vince lactam is a moderate preferable substrate Rhodococcus erythropolis R4 (-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.4 60
-
-
Rhodococcus erythropolis
3.5.2.B2 60
-
-
Rhodococcus erythropolis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.4 50
-
1 h, the enzyme maintains 100% of its original activity when incubated for 1 h Rhodococcus erythropolis
3.5.2.B2 50
-
1 h, the enzyme can maintain 100% of its original activity when incubated for 1 h Rhodococcus erythropolis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.4 2.1
-
Acrylamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 20.2
-
acetamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 155.2
-
Propionamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 157.7
-
Benzamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.2.B2 78
-
2-azabicyclo[2.2.1]hept-5-en-3-one pH and temperature not specified in the publication Rhodococcus erythropolis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.4 9
-
-
Rhodococcus erythropolis
3.5.2.B2 9
-
-
Rhodococcus erythropolis

General Information

EC Number General Information Comment Organism
3.5.1.4 metabolism the enzyme is involved in the nitrile hydratase pathway Rhodococcus erythropolis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.4 0.087
-
Acrylamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 1.14
-
acetamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 4.54
-
Propionamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.1.4 153.5
-
Benzamide pH and temperature not specified in the publication Rhodococcus erythropolis
3.5.2.B2 1.45
-
2-azabicyclo[2.2.1]hept-5-en-3-one pH and temperature not specified in the publication Rhodococcus erythropolis