2009
DOI: 10.1128/jb.00633-09
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Allosteric Regulation of Glucosamine-6-Phosphate Deaminase (NagB) and Growth ofEscherichia colion Glucosamine

Abstract: Growth on N-acetylglucosamine (GlcNAc) produces intracellular N-acetylglucosamine-6-phosphate (GlcNAc6P), which affects the regulation of the catabolism of amino sugars in Escherichia coli in two ways. First, GlcNAc6P is the inducing signal for the NagC repressor, and thus it increases the expression of the enzymes of the nagE-nagBACD operon. Second, it is the allosteric activator of glucosamine-6P (GlcN6P) deaminase, NagB, and thus increases the catalytic capacity of this key enzyme in the metabolism of amino… Show more

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Cited by 26 publications
(23 citation statements)
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References 34 publications
(40 reference statements)
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“…The enzyme under these conditions is operating at between 50 and 90% of its maximum rate. These values are consistent with the high NagB activity deduced for the enzyme during growth on GlcN (22).…”
Section: Resultssupporting
confidence: 78%
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“…The enzyme under these conditions is operating at between 50 and 90% of its maximum rate. These values are consistent with the high NagB activity deduced for the enzyme during growth on GlcN (22).…”
Section: Resultssupporting
confidence: 78%
“…The nagE-BA genes, controlled by the GlcNAc6P-sensitive NagC repressor, are partially induced by growth on GlcN (22,30), This low-level induction supports the idea that some GlcNAc6P is formed during growth on GlcN but also implies that it is only present in a low concentration.…”
supporting
confidence: 56%
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“…The repressor activity of NagC depends on its binding to palindromic dre (for DasR responsive element) (9,10) sites in the promoter regions of the target genes. When GlcNAc is present in the environment, intracellular GlcNAc-6-P accumulates and activates the expression of genes for GlcNAc and GlcN catabolism by disrupting the interaction between NagC and dre sites (5,(11)(12)(13). In the Gram-positive bacterium Bacillus subtilis, a GntR/HutC-type regulator, designated NagR (formerly YvoA), binds to nonhomologous operator sites, also called dre (14,15), to control the transcription of nagA, nagB, and nagP, which codes for a GlcNAc-specific PTS permease.…”
mentioning
confidence: 99%