Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme
about
X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoateAcetohydroxyacid synthases: evolution, structure, and function.Molecular and chemical dialogues in bacteria-protozoa interactions.Molecular evolution of acetohydroxyacid synthase in bacteria.The minimum activation peptide from ilvH can activate the catalytic subunit of AHAS from different species.
P2860
Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme
description
2008 nî lūn-bûn
@nan
2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@ast
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@en
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@nl
type
label
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@ast
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@en
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@nl
prefLabel
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@ast
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@en
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@nl
P356
P1433
P1476
Escherichia coli ilvN interact ...... nd activates the AHAS I enzyme
@en
P2093
Ashima Mitra
Siddhartha P Sarma
P304
P356
10.1021/BI701893B
P407
P577
2008-02-12T00:00:00Z