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Items: 1 to 20 of 22

1.
The Tertiary Origin of the Allosteric Activation of E. coli Glucosamine-6-Phosphate Deaminase Studied by Sol-Gel Nanoencapsulation of Its T Conformer
Sergio Zonszein, Laura I. Álvarez-Añorve, Roberto J. Vázquez-Núñez, Mario L. Calcagno
PLoS One. 2014; 9(5): e96536. Published online 2014 May 2. doi: 10.1371/journal.pone.0096536
PMCID:
PMC4008608
AbstractArticlePDF–1.0M
2.
Allosteric Regulation of Glucosamine-6-Phosphate Deaminase (NagB) and Growth of Escherichia coli on Glucosamine
Laura I. Álvarez-Añorve, Ismael Bustos-Jaimes, Mario L. Calcagno, Jacqueline Plumbridge
J Bacteriol. 2009 Oct; 191(20): 6401–6407. Published online 2009 Aug 21. doi: 10.1128/JB.00633-09
PMCID:
PMC2753035
AbstractArticlePDF–897K
3.
Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides.
M M Altamirano, J A Plumbridge, H A Barba, M L Calcagno
Biochem J. 1993 Nov 1; 295(Pt 3): 645–648. doi: 10.1042/bj2950645
PMCID:
PMC1134607
SummaryPage BrowsePDF–777K
4.
Amino Sugar Assimilation by Escherichia coli
James P. Rolls, C. W. Shuster
J Bacteriol. 1972 Nov; 112(2): 894–902. doi: 10.1128/jb.112.2.894-902.1972
PMCID:
PMC251501
SummaryPage BrowsePDF–1.3M
5.
Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars
R. J. White
Biochem J. 1968 Feb; 106(4): 847–858. doi: 10.1042/bj1060847
PMCID:
PMC1198589
SummaryPage BrowsePDF–1.6M
6.
The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli
R. J. White, C. A. Pasternak
Biochem J. 1967 Oct; 105(1): 121–125. doi: 10.1042/bj1050121
PMCID:
PMC1198282
SummaryPage BrowsePDF–740K
7.
Mutations Affecting Amino Sugar Metabolism in Escherichia coli K-12
R. P. Holmes, R. R. B. Russell
J Bacteriol. 1972 Jul; 111(1): 290–291. doi: 10.1128/jb.111.1.290-291.1972
PMCID:
PMC251271
SummaryPage BrowsePDF–230K
8.
Coordinated regulation of amino sugar-synthesizing and -degrading enzymes in Escherichia coli K-12.
J A Plumbridge, O Cochet, J M Souza, M M Altamirano, M L Calcagno, B Badet
J Bacteriol. 1993 Aug; 175(16): 4951–4956. doi: 10.1128/jb.175.16.4951-4956.1993
PMCID:
PMC204958
SummaryPage BrowsePDF–1.5M
9.
The Nitrogen Regulatory PII Protein (GlnB) and N-Acetylglucosamine 6-Phosphate Epimerase (NanE) Allosterically Activate Glucosamine 6-Phosphate Deaminase (NagB) in Escherichia coli
Irina A. Rodionova, Norman Goodacre, Mohan Babu, Andrew Emili, Peter Uetz, Milton H. Saier, Jr.
J Bacteriol. 2018 Mar 1; 200(5): e00691-17. Prepublished online 2017 Dec 11. Published online 2018 Feb 7. doi: 10.1128/JB.00691-17
PMCID:
PMC5809692
AbstractArticlePDF–1.6M
10.
An examination of the inhibitory effects of N-iodoacetylglucosamine on Escherichia coli and isolation of resistant mutants
R. J. White, P. W. Kent
Biochem J. 1970 Jun; 118(1): 81–87. doi: 10.1042/bj1180081
PMCID:
PMC1179083
SummaryPage BrowsePDF–1.1M
11.
Why Does Escherichia coli Grow More Slowly on Glucosamine than on N-Acetylglucosamine? Effects of Enzyme Levels and Allosteric Activation of GlcN6P Deaminase (NagB) on Growth Rates
Laura I. Álvarez-Añorve, Mario L. Calcagno, Jacqueline Plumbridge
J Bacteriol. 2005 May; 187(9): 2974–2982. doi: 10.1128/JB.187.9.2974-2982.2005
PMCID:
PMC1082822
AbstractArticlePDF–157K
12.
Induction of the nag regulon of Escherichia coli by N-acetylglucosamine and glucosamine: role of the cyclic AMP-catabolite activator protein complex in expression of the regulon.
J A Plumbridge
J Bacteriol. 1990 May; 172(5): 2728–2735. doi: 10.1128/jb.172.5.2728-2735.1990
PMCID:
PMC208918
SummaryPage BrowsePDF–1.8M
13.
DNA bending and expression of the divergent nagE-B operons.
J Plumbridge, A Kolb
Nucleic Acids Res. 1998 Mar 1; 26(5): 1254–1260. doi: 10.1093/nar/26.5.1254
PMCID:
PMC147383
SummaryPDF–243K
14.
Alternative route for biosynthesis of amino sugars in Escherichia coli K-12 mutants by means of a catabolic isomerase.
A P Vogler, S Trentmann, J W Lengeler
J Bacteriol. 1989 Dec; 171(12): 6586–6592. doi: 10.1128/jb.171.12.6586-6592.1989
Correction in:
J Bacteriol. 1990 Sep; 172(9): 5521.
PMCID:
PMC210551
SummaryPage BrowsePDF–1.3M
15.
How to achieve constitutive expression of a gene within an inducible operon: the example of the nagC gene of Escherichia coli.
J Plumbridge
J Bacteriol. 1996 May; 178(9): 2629–2636. doi: 10.1128/jb.178.9.2629-2636.1996
PMCID:
PMC177988
SummaryPDF–388K
16.
Identification of a Dedicated Recycling Pathway for Anhydro-N-Acetylmuramic Acid and N-Acetylglucosamine Derived from Escherichia coli Cell Wall Murein
James T. Park
J Bacteriol. 2001 Jul; 183(13): 3842–3847. doi: 10.1128/JB.183.13.3842-3847.2001
PMCID:
PMC95265
AbstractArticlePDF–93K
17.
The phosphocarrier protein HPr of the bacterial phosphotransferase system globally regulates energy metabolism by directly interacting with multiple enzymes in Escherichia coli
Irina A. Rodionova, Zhongge Zhang, Jitender Mehla, Norman Goodacre, Mohan Babu, Andrew Emili, Peter Uetz, Milton H. Saier, Jr.
J Biol Chem. 2017 Aug 25; 292(34): 14250–14257. Published online 2017 Jun 20. doi: 10.1074/jbc.M117.795294
PMCID:
PMC5572926
AbstractArticlePDF–877K
18.
DNA binding sites for the Mlc and NagC proteins: regulation of nagE, encoding the N-acetylglucosamine-specific transporter in Escherichia coli
Jacqueline Plumbridge
Nucleic Acids Res. 2001 Jan 15; 29(2): 506–514. doi: 10.1093/nar/29.2.506
PMCID:
PMC29661
AbstractArticlePDF–1.1M
19.
Factors Influencing the Identification of Transcription Factor Binding Sites by Cross-Species Comparison
Lee Ann McCue, William Thompson, C. Steven Carmack, Charles E. Lawrence
Genome Res. 2002 Oct; 12(10): 1523–1532. doi: 10.1101/gr.323602
PMCID:
PMC187528
AbstractArticlePDF–192K
20.
Protein abundance profiling of the Escherichia coli cytosol
Yasushi Ishihama, Thorsten Schmidt, Juri Rappsilber, Matthias Mann, F Ulrich Hartl, Michael J Kerner, Dmitrij Frishman
BMC Genomics. 2008; 9: 102. Published online 2008 Feb 27. doi: 10.1186/1471-2164-9-102
PMCID:
PMC2292177
AbstractArticlePDF–1.0M

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