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The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.

Aspartate transcarbamoylase from Escherichia coli shows homotropic cooperativity for aspartate as well as heterotropic regulation by nucleotides. Structurally, it consists of two trimeric catalytic subunits and three dimeric regulatory subunits, each chain being comprised of two domains. Glu-50 and...

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Библиографические подробности
Главные авторы: Baker, D. P., Fetler, L., Vachette, P., Kantrowitz, E. R.
Формат: Artigo
Язык:Inglês
Опубликовано: Cold Spring Harbor Laboratory Press 1996
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143294/
https://ncbi.nlm.nih.gov/pubmed/8931146
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