Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase.

Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase.

Item
http://www.wikidata.org/entity/Q31492804
Summarizing and exploring data of a decade of cytokinin-related transcriptomicsTransient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector bindingThe ACR11 encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with GLN2 in Arabidopsis.Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers.Molecular characterization of a novel gene family encoding ACT domain repeat proteins in Arabidopsis.Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.Reply: The BIF Domain Is Structurally and Functionally Distinct from Other Types of ACT-Like Domains.Characterization of the 2-hydroxy-acid dehydrogenase McyI, encoded within the microcystin biosynthesis gene cluster of Microcystis aeruginosa PCC7806.
P2860

Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase.

Item
http://www.wikidata.org/entity/Q31492804
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@ast
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@en
type
label
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@ast
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@en
prefLabel
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@ast
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Specific interactions at the r ...... hosphoglycerate dehydrogenase.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698