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[protein]-Npi-phospho-L-histidine + 2',3'-epoxypropyl beta-D-glucopyranoside
?
-
pseudosubstrate
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose[side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + chloroacetyl beta-D-glucopyranoside
?
-
pseudosubstrate
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucopyranoside
[protein]-L-histidine + methyl alpha-D-glucopyranoside 6-phosphate
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucoside[side 1]
[protein]-L-histidine + methyl alpha-D-glucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + methyl alpha-glucoside[side 1]
[protein]-L-histidine + methyl alpha-glucoside 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + methyl-alpha-D-glucopyranoside
?
-
-
-
-
?
additional information
?
-
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose[side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose[side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 6-phosphate[side 2]
-
the reaction occurs with high sugar concentrations in vitro
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 6-phosphate[side 2]
-
the reaction occurs with high sugar concentrations in vitro
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
722181, 735474, 736043, 736334, 736345, 736353, 736356, 736394, 736401, 736758, 736764, 736823, 737178, 760637 -
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
the enzyme is highly stereoselective for its substrate D-glucose
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
high specificity for D-glucose
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
the reaction occurs with high sugar concentrations in vitro
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
the reaction occurs with high sugar concentrations in vitro
-
-
?
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucoside[side 1]
[protein]-L-histidine + methyl alpha-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucoside[side 1]
[protein]-L-histidine + methyl alpha-D-glucose 6-phosphate[side 2]
-
-
-
-
?
additional information
?
-
-
the wild type enzyme does not transport D-ribose
-
-
?
additional information
?
-
the enzyme does not bind L-glucose
-
-
-
additional information
?
-
-
the enzyme does not bind L-glucose
-
-
-
additional information
?
-
-
no activity with D-fructose
-
-
?
additional information
?
-
-
no activity with D-fructose
-
-
?
additional information
?
-
-
natural mono- or disaccharides, such as mannose or N-acetylglucosamine are not phosphorylated by either isoform EIICBAGlc1 nor EIICBAGlc2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucoside[side 1]
[protein]-L-histidine + methyl alpha-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
722181, 735474, 736043, 736334, 736345, 736353, 736356, 736394, 736401, 736758, 736764, 736823, 737178, 760637 -
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
the enzyme is highly stereoselective for its substrate D-glucose
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
high specificity for D-glucose
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bachem, S.; Faires, N.; Stulke, J.
Characterization of the presumptive phosphorylation sites of the Bacillus subtilis glucose permease by site-directed mutagenesis: implication in glucose transport and catabolite repression
FEMS Microbiol. Lett.
156
233-238
1997
Bacillus subtilis, Bacillus subtilis 168
brenda
Gabor, E.; Goehler, A.K.; Kosfeld, A.; Staab, A.; Kremling, A.; Jahreis, K.
The phosphoenolpyruvate-dependent glucose-phosphotransferase system from Escherichia coli K-12 as the center of a network regulating carbohydrate flux in the cell
Eur. J. Cell Biol.
90
711-720
2011
Escherichia coli
brenda
Chatterjee, R.; Millard, C.S.; Champion, K.; Clark, D.P.; Donnelly, M.I.
Mutation of the ptsG gene results in increased production of succinate in fermentation of glucose by Escherichia coli
Appl. Environ. Microbiol.
67
148-154
2001
Escherichia coli, Escherichia coli NZN111
brenda
Robillard, G.T.; Beechey, R.B.
Evidence for the existence of a channel in the glucose-specific carrier EIIGlc of the Salmonella typhimurium phosphoenolpyruvate-dependent phosphotransferase system
Biochemistry
25
1346-1354
1986
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Garcia-Alles, L.F.; Navdaeva, V.; Haenni, S.; Erni, B.
The glucose-specific carrier of the Escherichia coli phosphotransferase system
Eur. J. Biochem.
269
4969-4980
2002
Escherichia coli
brenda
Liberman, E.S.; Bleiweis, A.S.
Glucose phosphoenolpyruvate-dependent phosphotransferase system of Streptococcus mutans GS5 studied by using cell-free extracts
Infect. Immun.
44
486-492
1984
Streptococcus mutans, Streptococcus mutans GS5
brenda
Ruyter, G.J.; Postma, P.W.; van Dam, K.
Control of glucose metabolism by enzyme IIGlc of the phosphoenolpyruvate-dependent phosphotransferase system in Escherichia coli
J. Bacteriol.
173
6184-6191
1991
Escherichia coli
brenda
Zeppenfeld, T.; Larisch, C.; Lengeler, J.W.; Jahreis, K.
Glucose transporter mutants of Escherichia coli K-12 with changes in substrate recognition of IICBGlc and induction behavior of the ptsG gene
J. Bacteriol.
182
4443-4452
2000
Escherichia coli
brenda
Becker, A.K.; Zeppenfeld, T.; Staab, A.; Seitz, S.; Boos, W.; Morita, T.; Aiba, H.; Mahr, K.; Titgemeyer, F.; Jahreis, K.
YeeI, a novel protein involved in modulation of the activity of the glucose-phosphotransferase system in Escherichia coli K-12
J. Bacteriol.
188
5439-5449
2006
Escherichia coli
brenda
Goehler, A.K.; Staab, A.; Gabor, E.; Homann, K.; Klang, E.; Kosfeld, A.; Muus, J.E.; Wulftange, J.S.; Jahreis, K.
Characterization of MtfA, a novel regulatory output signal protein of the glucose-phosphotransferase system in Escherichia coli K-12
J. Bacteriol.
194
1024-1035
2012
Escherichia coli
brenda
Stock, J.; Waygood, E.; Meadow, N.; Postma, P.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. The glucose receptors of the Salmonella typhimurium phosphotransferase system
J. Biol. Chem.
257
14543-14552
1982
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium SB3507
brenda
Erni, B.; Zanolari, B.
Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc
J. Biol. Chem.
261
16398-16403
1986
Escherichia coli (P69786)
brenda
Buhr, A.; Fluekiger, K.; Erni, B.
The glucose transporter of Escherichia coli. Overexpression, purification, and characterization of functional domains
J. Biol. Chem.
269
23437-23443
1994
Escherichia coli (P69786), Escherichia coli
brenda
Oh, H.; Park, Y.; Park, C.
A mutated PtsG, the glucose transporter, allows uptake of D-ribose
J. Biol. Chem.
274
14006-14011
1999
Escherichia coli
brenda
Jeong, J.Y.; Kim, Y.J.; Cho, N.; Shin, D.; Nam, T.W.; Ryu, S.; Seok, Y.J.
Expression of ptsG encoding the major glucose transporter is regulated by ArcA in Escherichia coli
J. Biol. Chem.
279
38513-38518
2004
Escherichia coli
brenda
Subhadra, B.; Lee, J.K.
Elucidation of the regulation of ethanol catabolic genes and ptsG using a glxR and adenylate cyclase gene (cyaB) deletion mutants of Corynebacterium glutamicum ATCC 13032
J. Microbiol. Biotechnol.
23
1683-1690
2013
Corynebacterium glutamicum (Q46072), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q46072), Corynebacterium glutamicum ATCC 13032
brenda
Yoon, K.; Lee, K.; Lee, J.; Park, S.
Cloning, nucleotide sequencing, and characterization of the ptsG gene encoding glucose-specific enzyme II of the phosphotransferase system from Brevibacterium lactofermentum
J. Microbiol. Biotechnol.
9
582-588
1999
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13869
-
brenda
Cabrera-Valladares, N.; Martinez, L.M.; Flores, N.; Hernandez-Chavez, G.; Martinez, A.; Bolivar, F.; Gosset, G.
Physiologic consequences of glucose transport and phosphoenolpyruvate node modifications in Bacillus subtilis 168
J. Mol. Microbiol. Biotechnol.
22
177-197
2012
Bacillus subtilis, Bacillus subtilis 168
brenda
Christiansen, I.; Hengstenberg, W.
Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system - two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?
Microbiology
145
2881-2889
1999
Staphylococcus carnosus
brenda
Knezevic, I.; Bachem, S.; Sickmann, A.; Meyer, H.E.; Stuelke, J.; Hengstenberg, W.
Regulation of the glucose-specific phosphotransferase system (PTS) of Staphylococcus carnosus by the antiterminator protein GlcT
Microbiology
146
2333-2342
2000
Staphylococcus carnosus
brenda
Plumbridge, J.
A mutation which affects both the specificity of PtsG sugar transport and the regulation of ptsG expression by Mlc in Escherichia coli
Microbiology
146
2655-2663
2000
Escherichia coli, Escherichia coli JM2053
brenda
Andre, A.; Maccheroni, W.; Doignon, F.; Garnier, M.; Renaudin, J.
Glucose and trehalose PTS permeases of Spiroplasma citri probably share a single IIA domain, enabling the spiroplasma to adapt quickly to carbohydrate changes in its environment
Microbiology
149
2687-2696
2003
Spiroplasma citri
brenda
Aboulwafa, M.; Chung, Y.J.; Wai, H.H.; Saier, M.H.
Studies on the Escherichia coli glucose-specific permease, PtsG, with a point mutation in its N-terminal amphipathic leader sequence
Microbiology
149
763-771
2003
Escherichia coli, Escherichia coli HK2240
brenda
Gaurivaud, P.; Persson, A.; Grand, D.L.; Westberg, J.; Solsona, M.; Johansson, K.E.; Poumarat, F.
Variability of a glucose phosphotransferase system permease in Mycoplasma mycoides subsp. mycoides Small Colony
Microbiology
150
4009-4022
2004
Mycoplasma mycoides, Mycoplasma mycoides PG1
brenda
Plumbridge, J.
Expression of ptsG, the gene for the major glucose PTS transporter in Escherichia coli, is repressed by Mlc and induced by growth on glucose
Mol. Microbiol.
29
1053-1063
1998
Escherichia coli
brenda
Gonzy-Treboul, G.; de Waard, J.H.; Zagorec, M.; Postma, P.W.
The glucose permease of the phosphotransferase system of Bacillus subtilis: evidence for IIGlc and IIIGlc domains
Mol. Microbiol.
5
1241-1249
1991
Bacillus subtilis
brenda
Bouma, C.L.; Meadow, N.D.; Stover, E.W.; Roseman, S.
II-BGlc, a glucose receptor of the bacterial phosphotransferase system: molecular cloning of ptsG and purification of the receptor from an overproducing strain of Escherichia coli
Proc. Natl. Acad. Sci. USA
84
930-934
1987
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kornberg, H.L.; Lambourne, L.T.; Sproul, A.A.
Facilitated diffusion of fructose via the phosphoenolpyruvate/glucose phosphotransferase system of Escherichia coli
Proc. Natl. Acad. Sci. USA
97
1808-1812
2000
Escherichia coli, Escherichia coli HK 2190
brenda
Garcia De Gonzalo, C.V.; Denham, E.L.; Mars, R.A.; Stuelke, J.; van der Donk, W.A.; van Dijl, J.M.
The phosphoenolpyruvate sugar phosphotransferase system is involved in sensitivity to the glucosylated bacteriocin sublancin
Antimicrob. Agents Chemother.
59
6844-6854
2015
Bacillus subtilis
brenda
Jeckelmann, J.M.; Erni, B.
The mannose phosphotransferase system (Man-PTS) - mannose transporter and receptor for bacteriocins and bacteriophages
Biochim. Biophys. Acta Biomembr.
1862
183412
2020
Escherichia coli
brenda
Xu, J.; Zhang, J.; Liu, D.; Zhang, W.
Increased glucose utilization and cell growth of Corynebacterium glutamicum by modifying the glucose-specific phosphotransferase system (PTSGlc) genes
Can. J. Microbiol.
62
983-992
2016
Corynebacterium glutamicum, Corynebacterium glutamicum XQ-8
brenda
Kim, H.J.; Jeong, H.; Lee, S.J.
Short-term adaptation modulates anaerobic metabolic flux to succinate by activating ExuT, a novel D-glucose transporter in Escherichia coli
Front. Microbiol.
11
27
2020
Escherichia coli
brenda
Kalbermatter, D.; Chiu, P.L.; Jeckelmann, J.M.; Ucurum, Z.; Walz, T.; Fotiadis, D.
Electron crystallography reveals that substrate release from the PTS IIC glucose transporter is coupled to a subtle conformational change
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