Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding
about
Subdomain II of α-isopropylmalate synthase is essential for activity: inferring a mechanism of feedback inhibition.Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily.
P2860
Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding
description
2012 nî lūn-bûn
@nan
2012 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մարտին հրատարակված գիտական հոդված
@hy
2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Removal of the C-terminal regu ...... s functional substrate binding
@ast
Removal of the C-terminal regu ...... s functional substrate binding
@en
Removal of the C-terminal regu ...... s functional substrate binding
@nl
type
label
Removal of the C-terminal regu ...... s functional substrate binding
@ast
Removal of the C-terminal regu ...... s functional substrate binding
@en
Removal of the C-terminal regu ...... s functional substrate binding
@nl
prefLabel
Removal of the C-terminal regu ...... s functional substrate binding
@ast
Removal of the C-terminal regu ...... s functional substrate binding
@en
Removal of the C-terminal regu ...... s functional substrate binding
@nl
P2093
P50
P356
P1433
P1476
Removal of the C-terminal regu ...... s functional substrate binding
@en
P2093
Esther M M Bulloch
Frances H A Huisman
Heather M Baker
Nayden Koon
P304
P356
10.1021/BI201717J
P407
P577
2012-03-20T00:00:00Z