Literature summary 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.

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.5.1.77	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
3.5.1.77	V40A	2fold increased activity, improvement in expression levels, mutation mainly gives rise to the increase in oxidative stability rather than thermostability	Agrobacterium tumefaciens

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.77	Agrobacterium tumefaciens	-	NRRL B11291	-
3.5.1.77	Agrobacterium tumefaciens NRRL B11291	-	NRRL B11291	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.5.1.77	-	Agrobacterium tumefaciens

Substrates and Products (Substrate)

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)