The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition
about
Direct binding targets of the stringent response alarmone (p)ppGppMaximizing efficiency of rumen microbial protein productionCrystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-β-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domainsDiscovery of novel nitrobenzothiazole inhibitors for Mycobacterium tuberculosis ATP phosphoribosyl transferase (HisG) through virtual screeningPhosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.Biosynthesis of Histidine.The ACT domain: a small molecule binding domain and its role as a common regulatory element.Systematic identification of conserved bacterial c-di-AMP receptor proteinsFrom cyanobacteria to plants: conservation of PII functions during plastid evolution.Uncoupling conformational states from activity in an allosteric enzyme.Substrate recognition by the hetero-octameric ATP phosphoribosyltransferase from Lactococcus lactis.Alterations in the two globular domains or in the connecting alpha-helix of bacterial ribosomal protein L9 induces +1 frameshifts.Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail.Histidine Regulates Seed Oil Deposition through Abscisic Acid Biosynthesis and β-Oxidation.Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog.A dimeric catalytic core relates the short and long forms of ATP-phosphoribosyltransferase.Independent catalysis of the short form HisG from Lactococcus lactis.ATP phosphoribosyltransferase from symbiont Entomomyces delphacidicola invovled in histidine biosynthesis of Nilaparvata lugens (Stål).
P2860
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P2860
The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition
description
2004 nî lūn-bûn
@nan
2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The structure of Escherichia c ...... tes and mode of AMP inhibition
@ast
The structure of Escherichia c ...... tes and mode of AMP inhibition
@en
The structure of Escherichia c ...... tes and mode of AMP inhibition
@nl
type
label
The structure of Escherichia c ...... tes and mode of AMP inhibition
@ast
The structure of Escherichia c ...... tes and mode of AMP inhibition
@en
The structure of Escherichia c ...... tes and mode of AMP inhibition
@nl
prefLabel
The structure of Escherichia c ...... tes and mode of AMP inhibition
@ast
The structure of Escherichia c ...... tes and mode of AMP inhibition
@en
The structure of Escherichia c ...... tes and mode of AMP inhibition
@nl
P2093
P1476
The structure of Escherichia c ...... tes and mode of AMP inhibition
@en
P2093
Gerry McDermott
John R Coggins
Samantha A Campbell
P304
P356
10.1016/J.JMB.2003.12.020
P407
P577
2004-02-06T00:00:00Z