Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.

doi:10.1021/bi00467a018

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Article

Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.

Biochemistry - 17 Apr 1990

Dembowski N J, Newton C J, Kantrowitz E R

Abstract excerpt

Structural studies of Escherichia coli aspartate transcarbamoylase suggest that the R state of the enzyme is stabilized by an interaction between Ser-171 of the aspartate domain and both the backbone carbonyl of His-134 and the side chain of Gln-133 of the carbamoyl phosphate domain of a catalyti...

Topics

Aspartate Carbamoyltransferase
Aspartic Acid
Binding Sites
Catalysis
Escherichia coli
Kinetics
Mutation
Phosphonoacetic Acid
Protein Conformation
Serine
Structure-Activity Relationship
Substrate Specificity

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