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Literature summary for 3.5.1.77 extracted from

  • Park, H.; Oh, K.; Kim, H.
    Improving the functional expression of N-carbamoylase by directed evolution using the green fluorescent protein fusion reporter system (2004), Methods Enzymol., 388, 187-195.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
T262A 1.5fold increased activity, improvement in expression levels, mutation results in a significant improvement in both oxidative stability and thermostability, increases stability of N-carbamoylase in vivo, thereby preventing it from degradation by cellular proteases Agrobacterium tumefaciens
V40A 2fold increased activity, improvement in expression levels, mutation mainly gives rise to the increase in oxidative stability rather than thermostability Agrobacterium tumefaciens

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
-
NRRL B11291
-
Agrobacterium tumefaciens NRRL B11291
-
NRRL B11291
-

Purification (Commentary)

Purification (Comment) Organism
-
Agrobacterium tumefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-carbamoyl-D-hydroxyphenylglycine + H2O
-
Agrobacterium tumefaciens D-hydroxyphenylglycine + NH3 + CO2
-
?
N-carbamoyl-D-hydroxyphenylglycine + H2O
-
Agrobacterium tumefaciens NRRL B11291 D-hydroxyphenylglycine + NH3 + CO2
-
?