The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity
about
Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseReplacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylaseThe first high pH structure ofEscherichia coliaspartate transcarbamoylaseStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseImportance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.
P2860
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity
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1999 nî lūn-bûn
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The 80s loop of the catalytic ...... s and homotropic cooperativity
@ast
The 80s loop of the catalytic ...... s and homotropic cooperativity
@en
type
label
The 80s loop of the catalytic ...... s and homotropic cooperativity
@ast
The 80s loop of the catalytic ...... s and homotropic cooperativity
@en
prefLabel
The 80s loop of the catalytic ...... s and homotropic cooperativity
@ast
The 80s loop of the catalytic ...... s and homotropic cooperativity
@en
P2093
P2860
P356
P1433
P1476
The 80s loop of the catalytic ...... s and homotropic cooperativity
@en
P2093
P2860
P304
P356
10.1110/PS.8.6.1305
P577
1999-06-01T00:00:00Z