Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme
about
Protein phosphorylation and regulation of adaptive responses in bacteriaMutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolismNitrogen assimilation in Escherichia coli: putting molecular data into a systems perspectiveInactivation of gltB abolishes expression of the assimilatory nitrate reductase gene (nasB) in Pseudomonas putida KT2442The ACR11 encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with GLN2 in Arabidopsis.P(II) signal transduction proteins, pivotal players in microbial nitrogen controlCharacterization of Escherichia coli glnL mutations affecting nitrogen regulation.Localization of the glnD gene on a revised map of the 200-kilobase region of the Escherichia coli chromosome.Isocitrate dehydrogenase kinase/phosphatase: aceK alleles that express kinase but not phosphatase activity.Nucleotidylation, not phosphorylation, is the major source of the phosphotyrosine detected in enteric bacteria.Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase.The product of the nitrogen fixation regulatory gene nfrX of Azotobacter vinelandii is functionally and structurally homologous to the uridylyltransferase encoded by glnD in enteric bacteriaSynthetic lethality with the dut defect in Escherichia coli reveals layers of DNA damage of increasing complexity due to uracil incorporation.Metabolomics-driven quantitative analysis of ammonia assimilation in E. coli.Mutational analysis of the bacterial signal-transducing protein kinase/phosphatase nitrogen regulator II (NRII or NtrB).Nitrogen control in bacteria.Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein.Sensitivity and robustness in covalent modification cycles with a bifunctional converter enzyme.Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector.
P2860
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P2860
Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme
description
1983 nî lūn-bûn
@nan
1983 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1983 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1983年の論文
@ja
1983年論文
@yue
1983年論文
@zh-hant
1983年論文
@zh-hk
1983年論文
@zh-mo
1983年論文
@zh-tw
1983年论文
@wuu
name
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@ast
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@en
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@nl
type
label
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@ast
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@en
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@nl
prefLabel
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@ast
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@en
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@nl
P1476
Cascade control of Escherichia ...... e and uridylyl-removing enzyme
@en
P2093
P304
P407
P577
1983-02-25T00:00:00Z