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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 catalytic chain [Ke, H.-M., Lipscomb, W.N., Cho, Y., & Honzatko, R. B. (1988) J. Mol. Biol. 204, 725-747]. In the present...

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Identifiers

PMID: 2111165
DOI: 10.1021/bi00467a018

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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