Information on EC 2.7.1.69 - protein-Npi-phosphohistidine-sugar phosphotransferase:
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EC NUMBERCOMMENTARY
2.7.1.69-

RECOMMENDED NAMEGeneOntology No.
protein-Npi-phosphohistidine-sugar phosphotransferaseGO:0009357

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
protein Npi-phospho-L-histidine + sugar = [protein]-L-histidine + sugar phosphate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phospho group transfer----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
protein-Npi-phospho-L-histidine:sugar Npi-phosphotransferaseEnzyme II of the phosphotransferase system. Comprises a group of related enzymes. The protein substrate is a phosphocarrier protein of low molecular mass (9.5 kDa). The protein is phosphorylated in a reaction catalysed by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase) and this acts as the phosphate donor for the above reaction. The enzyme translocates the sugar it phosphorylates into bacteria. Aldohexoses, and their glycosides and alditols, are phosphorylated on O-6, whereas fructose and sorbose are phosphorylated on O-1. Glycerone and disaccharides are also substrates.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
BglF protein----
EIImalStreptococcus mutans--674325
enzyme IIEscherichia coli--692830
enzyme II of the phosphotransferase system----
enzyme II protein of a phosphoenolpyruvate:sugar phosphotransferaseBifidobacterium breveA2Q6K5-671496
enzyme IIl4ac----
fructose EIICorynebacterium glutamicum--661794
gene bglC RNA formation factors----
gene glC proteins----
GlcPMycobacterium smegmatis--705222
glucose permease----
glucose permeaseRattus norvegicus--671780
glucose permeaseKluyveromyces lactis--673756
glucose permeaseMycobacterium smegmatis--705222
GLUT1Rattus norvegicus--671780
Hgt1Kluyveromyces lactis--673756
MalTStreptococcus mutans-maltose transporter674325
mannitol transport protein enzyme II mtl----
MSMEG4187Mycobacterium smegmatis--705222
PEP-dependent carbohydrate:phosphotransferase systemEscherichia coli--692830
PEP-dependent phosphotransferase enzyme II----
PEP-sugar phosphotransferase enzyme II----
phosphoenolpyruvate-dependent carbohydrate:phosphotransferase systemEscherichia coli--692830
phosphoenolpyruvate-dependent phosphotransferase systemStreptococcus mutans--674325
phosphoenolpyruvate-sugar phosphotransferase enzyme II----
phosphoenolpyruvate:sugar phosphotransferaseEscherichia coli--692830
phosphoenolpyruvate:sugar phosphotransferase system, glucose-specificLactobacillus casei--675849
phosphohistidinoprotein-hexose phosphoribosyltransferase----
phosphohistidinoprotein-hexose phosphotransferase----
phosphoprotein factor-hexose phosophotransferase----
phosphotransferase, phosphohistidinoprotein-hexose----
protein, specific or class, gene bglC----
PTSEscherichia coli--692830
PTS permease----
PtsGStreptococcus mutans--674325
ribonucleic acid formation factor, gene glC----
sucrose EIICorynebacterium glutamicum--661794
sucrose phosphotransferase system II----
mannose class phosphoenolpyruvate:sugar phosphotransferase systemLactobacillus casei--675497
additional informationEscherichia coli-enzyme II is part of the bacterial phosphoenolpyruvate:sugar phosphotransferase system in Escherichia coli692830

CAS REGISTRY NUMBERCOMMENTARY
37278-09-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus sp.-641860--Manually annotated by BRENDA team
Bacillus subtilis-641857, 641859, 641873, 641880--Manually annotated by BRENDA team
Bifidobacterium brevestrain UCC2003671496A2Q6K5SwissProtManually annotated by BRENDA team
Clostridium sp.-641860--Manually annotated by BRENDA team
Corynebacterium glutamicumstrain ATCC 13032661794--Manually annotated by BRENDA team
Enterococcus faecalis26487641872--Manually annotated by BRENDA team
Enterococcus faecalis 2648726487641872--Manually annotated by BRENDA team
Escherichia coli-641858, 641860, 641861, 641862, 641863, 641864, 641865, 641866, 641867, 641868, 641874, 641875, 641877, 641879, 641881, 641883, 641885, 641886, 641887, 641888, 692907--Manually annotated by BRENDA team
Escherichia coligene ptsI692830--Manually annotated by BRENDA team
Klebsiella pneumoniae-641878--Manually annotated by BRENDA team
Klebsiella sp.-641860--Manually annotated by BRENDA team
Kluyveromyces lactis-673756--Manually annotated by BRENDA team
Lactobacillus casei-675497, 675849--Manually annotated by BRENDA team
Lactobacillus sp.-641860--Manually annotated by BRENDA team
Mycobacterium smegmatisstrain MC2 155705222--Manually annotated by BRENDA team
Mycoplasma capricolum-641882--Manually annotated by BRENDA team
Mycoplasma sp.-641860--Manually annotated by BRENDA team
Rattus norvegicus-671780--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium-641860, 641869, 641870--Manually annotated by BRENDA team
Staphylococcus aureus-641860, 641876, 641889--Manually annotated by BRENDA team
Staphylococcus aureusstrain 305 A641871--Manually annotated by BRENDA team
Staphylococcus aureus 305 Astrain 305 A641871--Manually annotated by BRENDA team
Streptococcus mutans-674325--Manually annotated by BRENDA team
Streptococcus sp.-641860--Manually annotated by BRENDA team
Streptomyces coelicolor-641884--Manually annotated by BRENDA team
Streptomyces griseofuscus-641884--Manually annotated by BRENDA team
Streptomyces lividans-641884--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + phosphohistidine-containing protein2-deoxy-D-glucose 6-phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli--641885---
2-deoxy-D-glucose + phosphohistidine-containing protein2-deoxy-D-glucose 6-phosphate + histidine-containing protein
show the reaction diagram		Rattus norvegicus--671780--?
2-deoxy-D-glucose + phosphohistidine-containing protein2-deoxy-D-glucose 6-phosphate + histidine-containing protein
show the reaction diagram		Enterococcus faecalis--641872---
D-fructose + phosphohistidine-containing proteinD-fructose 1-phosphate + histidine-containing protein
show the reaction diagram		Corynebacterium glutamicum--661794--?
D-glucose + phosphohistidine-containing proteinD-glucose 6-phosphate + histidine-containing protein
show the reaction diagram		Rattus norvegicus--671780--?
D-glucose + phosphohistidine-containing proteinD-glucose 6-phosphate + histidine-containing protein
show the reaction diagram		Lactobacillus casei--675849--?
D-glucose + phosphohistidine-containing protein?
show the reaction diagram		Mycobacterium smegmatis-the MSMEG4187 glucose permease is a high affinity glucose-specific permease705222--?
methyl-alpha-D-glucoside + D-glucose 6-phosphatemethyl-alpha-D-glucoside 6-phosphate + D-glucose
show the reaction diagram		Escherichia coli--641885, 641888---
phosphoenolpyruvate + protein histidinepyruvate + protein phospho-L-histidine
show the reaction diagram		Escherichia coli-in the PTS system, HPr interacts with a number of evolutionarily unrelated proteins, mainly, it delivers phosphoryl groups from enzyme I, EI, to the sugar-specific transporters, EIIs, overview, the dimeric protein EI is phosphorylated, the phosphogroup is transferred to the sugar-specific transporter EII by HPr692830--?
sucrose + phosphohistidine-containing proteinsucrose 6-phosphate + histidine-containing protein
show the reaction diagram		Corynebacterium glutamicum--661794--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium--641870--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Bacillus subtilis--641857, 641859--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli--641858, 641865, 641877, 641886, 641887--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Lactobacillus casei--675497--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Klebsiella sp.--641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Streptococcus mutans--674325--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Mycoplasma capricolum--641882--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Bifidobacterium breveA2Q6K5-671496--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium--641860glucose is phosphorylated at position 6641860?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium-glucose-specific enzyme catalyzes the phosphoenolpyruvate-dependent phosphorylation of methyl-alpha-D-glucopyranoside641869-641869?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-isoenzyme EIIGlc phosphorylates:glucose, 1-deoxy-D-glucose with 119% of the activity with glucose,alpha-1-fluoro-D-glucose at 98% of the activity with D-glucose, beta-1-fluoro-D-glucose at 112% of the activity with D-glucose, mannose at 5% of the activity with D-glucose, 2-deoxy-D-glucose at 17% of the activity with D-glucose, 2-fluoro-D-glucose at 18% of the activity with D-glucose, allose at 3% of the activity with D-glucose, 3-deoxy-D-glucose at 8% of the activity with D-glucose, 3-fluoro-D-glucose at 53% of the activity with D-glucose, 4-deoxy-D-glucose at 2% of the activity with D-glucose, 4-fluoro-D-glucose at 7% of the activity with D-glucose. EIIMan phosphorylates: glucose, 1-deoxy-D-glucose with 42% of the activity with glucose, alpha -1-fluoro-D-glucose at 79% of the activity with D-glucose, beta-1-fluoro-D-glucose at 102% of the activity with D-glucose, mannose at 169% of the activity with D-glucose, 2-deoxy-D-glucose at 120% of the activity with D-glucose, 2-fluoro-D-glucose at 120% of the activity with D-glucose, allose at 9% of the activity with D-glucose, 3-deoxy-D-glucose at 34% of the activity with D-glucose, 3-fluoro-D-glucose at 91% of the activity with D-glucose, 4-deoxy-D-glucose at 0.3% of the activity with D-glucose, 4-fluoro-D-glucose at 5% of the activity with D-glucose641885--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-mannitol-specific enzyme, reaction with mannitol and mannitol 1-phosphate641863--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Bacillus subtilis-phosphorylation of glucose641873--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Enterococcus faecalis-phosphorylation of glucose641872glucose is phosphorylated at position 6641872?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-mannitol-specific enzyme641868, 641879--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-mannitol-specific enzyme641867mannitol is phosphorylated at position 1641867?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-methyl-alpha-glucoside. G320V mutation allows the isoenzyme EIIGlc to transport mannitol641888--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Staphylococcus aureus-phosphorylation of beta-galactosidase by the lactose phosphotransferase system641876--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Streptomyces coelicolor-fructose-specific enzyme II activity641884--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Streptomyces griseofuscus-fructose-specific enzyme II activity641884---
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Streptomyces lividans-fructose-specific enzyme II activity641884--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Lactobacillus sp.-isoenzyme IIglc is specific for glucose and alpha-methylglucopyranoside. Isoenzyjme IIlac is specific for lactose, lactulose and lactobionic acid. Isoenzyme IIxtl is specific for xylitol and D-arabitol. Isoenzyme IIgal is specific for galactose. Isoenzyme IIrtl is specific for ribitol641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Clostridium sp.-isoenzyme IIglc is specific for glucose. Isoenzyme IIfru is specific for fructose. Isoenzyme IIscr is specific for sucrose. Isoenzyme IImtl is specific for mannitol and sorbitol641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Mycoplasma sp.-isoenzyme IIglc is specific for glucose and alpha-methylglucopyranose641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-phosphoenolpyruvate-dependent and mannitol 1-phosphate-dependent phosphorylation of mannitol641874, 641875--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Staphylococcus aureus-galactoside-specific enzyme, reaction with o-nitrophenyl-beta-D-galactoside641871--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Bacillus sp.-Isoenzyme IImtl is specific for mannitol. Isoenzyme IIman is specific for mannose. Isoenzyme IIglc is specific for glucose and alpha-methylglucopyranoside. Isonzyme IItre is specific for trehalose641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-in the absence of beta-glucosides, the enzyme phosphorylates BglG, a positive regulator of bgl operon transcription, thus inactivating BglG. In the presence of beta-glucosides, it activates BglG by dephosphorylating it and, at the same time, transports beta-glucosides into the cell and phosphorylates them641883--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-enzyme IIMan, reaction with methyl alpha-glucoside641864--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Klebsiella pneumoniae-sorbose permease641878--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-N-acetylglucosamine641861--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-isoenzyme IIGlc enzyme, reaction with alpha-methylglucopyranoside641862--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Bacillus subtilis-fructose permease641880--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-mannitol-specific enzyme catalyzes both the phosphoenolpyruvate-dependent and the mannitol 1-phosphate-dependent phosphorylation of D-mannitol with high specificity for the accepting sugar and the phosphoryl donor641866--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-glucose permease, mannitol permease and mannose permease641881--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Streptococcus sp.-isoenzyme IIlac is specific for lactose, thiomethyl-beta-galactopyranoside and galactose. Isoenzyme IIglc is specific for glucose, 2-deoxyglucose and glucosamine. Isoenzyme IIgal is specific for galactose. Isoenzyme IIscr is specific for sucrose. Isoenzyme IIfru is specific for fructose641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Staphylococcus aureus-isoenzyme IIlac is specific for lactose and thiomethyl-beta-galactopyranoside641860--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-a group of sugar-specific enzymes, which, together with the soluble enzymes of the PTS (phosphoenolpyruvate, enzyme I (EC 2.7.3.9), and histidine-containing protein (HPr)), are responsible for the translocation of sugars across membranes641874--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Escherichia coli-a group of sugar-specific enzymes, which, together with the soluble enzymes of the PTS (phosphoenolpyruvate, enzyme I (EC 2.7.3.9), and histidine-containing protein (HPr)), are responsible for the translocation of sugars across membranes641860glucose is phosphorylated at position 6, fructose is phosphorylated at position 1641860?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Staphylococcus aureus-o-nitrophenyl-beta-D-galactopyranoside641889--?
sugar + phosphohistidine-containing proteinsugar phosphate + histidine-containing protein
show the reaction diagram		Kluyveromyces lactis-high affinity galactose transporter673756--?
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-in the absence of beta-glucosides, the enzyme phosphorylates BglG, a positive regulator of bgl operon transcription, thus inactivating BglG. In the presence of beta-glucosides, it activates BglG by dephosphorylating it and, at the same time, transports beta-glucosides into the cell and phosphorylates them641883---
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-inducible enzyme641875--?
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-part of the bacterial phosphotransferase system, EC 2.7.1.69 comprises a group of sugar-specific enzymes, which, together with the soluble enzymes of the PTS (phosphoenolpyruvate, enzyme I EC 2.7.3.9, and histidine-containing protein (HPr)), are responsible for the translocation of sugars across membranes641860, 641874--?
sugar + phosphohistidine-containing protein?
show the reaction diagram		Streptomyces coelicolor, Streptomyces lividans-fructose-specific enzyme IIfruc is fructose-inducible641884---
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-physiological functions of the mannitol enzyme II: 1. chemoreception, 2. unidirectional and exchange group translocation, 3. phosphoenolpyruvate-dependent and mannitol-1-phosphate-dependent sugar phosphorylation, 4. autoinduction of phosphotransferase system protein synthesis, 5. control of non-phosphotransferase-system permease activity, 6. control of adenylate cyclase activity641874--?
sugar + phosphohistidine-containing protein?
show the reaction diagram		Streptomyces griseofuscus-fructose-specific enzyme IIfruc is constitutively expressed641884---
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-the mannitol-specific enzyme is responsible for the transport and phosphorylation of D-mannitol641866--?
methyl-alpha-D-glucoside + D-glucose 6-phosphatemethyl-alpha-D-glucoside 6-phosphate + D-glucose
show the reaction diagram		Escherichia coli-transphosphorylation activity692907--?
additional information?-Escherichia coli-the enzyme catalyzes an exchange reaction in which a phosphoryl moiety is transferred from one molecule of the heat stable phosphocarrier protein Hpr to another641863---
additional information?-Escherichia coli-the histidine protein, HPr, is the energy-coupling protein of the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system, PTS, which catalyzes sugar transport in the bacterium692830---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
phosphoenolpyruvate + protein histidinepyruvate + protein phospho-L-histidine
show the reaction diagram		Escherichia coli-in the PTS system, HPr interacts with a number of evolutionarily unrelated proteins, mainly, it delivers phosphoryl groups from enzyme I, EI, to the sugar-specific transporters, EIIs, overview692830--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-in the absence of beta-glucosides, the enzyme phosphorylates BglG, a positive regulator of bgl operon transcription, thus inactivating BglG. In the presence of beta-glucosides, it activates BglG by dephosphorylating it and, at the same time, transports beta-glucosides into the cell and phosphorylates them641883--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-inducible enzyme641875--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-part of the bacterial phosphotransferase system, EC 2.7.1.69 comprises a group of sugar-specific enzymes, which, together with the soluble enzymes of the PTS (phosphoenolpyruvate, enzyme I EC 2.7.3.9, and histidine-containing protein (HPr)), are responsible for the translocation of sugars across membranes641860, 641874--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Streptomyces coelicolor, Streptomyces lividans-fructose-specific enzyme IIfruc is fructose-inducible641884--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-physiological functions of the mannitol enzyme II: 1. chemoreception, 2. unidirectional and exchange group translocation, 3. phosphoenolpyruvate-dependent and mannitol-1-phosphate-dependent sugar phosphorylation, 4. autoinduction of phosphotransferase system protein synthesis, 5. control of non-phosphotransferase-system permease activity, 6. control of adenylate cyclase activity641874--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Streptomyces griseofuscus-fructose-specific enzyme IIfruc is constitutively expressed641884--
sugar + phosphohistidine-containing protein?
show the reaction diagram		Escherichia coli-the mannitol-specific enzyme is responsible for the transport and phosphorylation of D-mannitol641866--
additional information?-Escherichia coli-the histidine protein, HPr, is the energy-coupling protein of the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system, PTS, which catalyzes sugar transport in the bacterium692830--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-(N-dansyl)aminoethyl-beta-D-thiogalactosideStaphylococcus aureus--641889 2D-image
5-thioglucoseEnterococcus faecalis--641872 2D-image
alpha-D-gluco-hexodialdo-1,5-pyranosideEscherichia coli--641885 2D-image
cytochalasin BRattus norvegicus--671780 2D-image
D-gluco-hexadialdo-1,5-pyranoseEscherichia coli-which exist as gem-diols in aqueous solution641885 2D-image
D-gluco-hexodialdo-1,5-pyranoseEscherichia coli--641885 2D-image
D-glucoseRattus norvegicus-noncompetitive inhibition671780 2D-image
D-glucose 6-phosphateEscherichia coli-monomeric fusion-protein of integral membrane subunit IICBGlc and malotose-binding protein exhibits no substrate inhibition although the oligomeric form does. Purification promotes subunit association, an increase in catalytic activity, and restoration of substrate inhibition692907 2D-image
DiethyldicarbonateEscherichia coli-inhibits exchange reaction641863 2D-image
ferricyanideEscherichia coli-inhibits glucose-specific enzyme, mannose-specific enzyme is less sensitive641864 2D-image
ferricyanideEscherichia coli-phosphorylated enzyme is less susceptible than non-phosphorylated enzyme641865 2D-image
forskolinRattus norvegicus--671780 2D-image
glucoseEscherichia coli--641885 2D-image
isopropyl-beta-D-thiogalactosideStaphylococcus aureus--641889 2D-image
mannitolEscherichia coli-strong substrate inhibition at neutral pH in the transphosphorylation reaction. No substrate inhibition for phosphoenolpyruvate-dependent reaction641866 2D-image
mannitolEscherichia coli--641888 2D-image
mannitol 1-phosphateEscherichia coli-strong substrate inhibition at neutral pH in the transphosphorylation reaction641866 2D-image
MannoseEnterococcus faecalis--641872 2D-image
methyl alpha-D-gluco-hexodialdo-1,5-pyranosideEscherichia coli-which exist as gem-diols in aqueous solution641885 2D-image
NEMEscherichia coli-inhibits phosphoenol-dependent phosphorylation of mannitol and mannitol 1-phosphate, no effect on activity of exchange reaction641863 2D-image
NEMEscherichia coli-enzyme reconstituted in phospholipid vesicles641867 2D-image
PCMBEscherichia coli-partial inactivation of exchange reaction641863 2D-image
phenazine methosulfateEscherichia coli-inhibits glucose-specific enzyme641864 2D-image
phenazine methosulfateEscherichia coli--641865 2D-image
PlumbaginEscherichia coli-inhibits glucose-specific enzyme641864 2D-image
PlumbaginEscherichia coli--641865 2D-image
SDSStaphylococcus aureus-complete inhibition complete inhibition of phosphorylation of beta-D-galactoside at 0.015% w/v, reversible, only slight inhibition of phosphorylation of methyl-alpha-D-glucoside641876 2D-image
Sodium deoxycholateStaphylococcus aureus-complete inhibition of phosphorylation of beta-D-galactoside at 0.33% w/v, reversible, only slight inhibition of phosphorylation of methyl-alpha-D-glucoside641876 2D-image
methyl alpha-D-glucopyranosideEscherichia coli--641885 2D-image
additional informationEscherichia coli-antibodies directed against the enzyme inhibit phosphoenolpyruvate-dependent activity to a greater extent than the transphosphorylation641866-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Lubrol PxEscherichia coli-purified enzyme is dependent on Lubrol PX and phospholipids for maximal activity641866 2D-image
phosphatidylglycerolSalmonella enterica subsp. enterica serovar Typhimurium-required for enzyme in sonicated suspension641869 2D-image
PhospholipidsEscherichia coli-purified enzyme is dependent on Lubrol PX and phospholipids for maximal activity641866-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.2-1-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
1.1-1-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
0.04-2-deoxy-D-glucoseEnterococcus faecalis-25°C641872 2D-image
0.49-2-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
1.5-2-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.45-2-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
1.2-2-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
2-3-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
4.1-3-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.49-3-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.61-3-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
4-4-deoxy-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
1.7-4-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
5-4-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
0.21-alpha-1-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.48-alpha-1-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
0.19-beta-1-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.47-beta-1-fluoro-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
0.019-D-glucoseMycobacterium smegmatis--705222 2D-image
0.04-D-glucoseEnterococcus faecalis-25°C641872 2D-image
0.22-D-glucoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.49-D-glucoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
3-D-glucoseRattus norvegicus--671780 2D-image
5-D-MannitolEscherichia coli-wild-type enzyme641888 2D-image
0.32-D-mannoseEscherichia coli-pH 7.5, enzyme EIIMan641885 2D-image
4.8-D-mannoseEscherichia coli-pH 7.5, enzyme EIIGlc641885 2D-image
0.011-mannitolEscherichia coli--641866 2D-image
0.023-methyl-alpha-D-glucopyranosideEscherichia coli-pH 7.5, 37°C, glucose-specific enzyme in presence of 3 mM ferrocyanide641864 2D-image
0.036-methyl-alpha-D-glucopyranosideEscherichia coli-pH 7.5, 37°C, glucose-specific enzyme in presence of 3 mM ferricyanide641864 2D-image
0.7-methyl-alpha-D-glucopyranosideEscherichia coli-pH 7.5, 37°C, mannose-specific enzyme in presence of 3 mM ferrocyanide641864 2D-image
1.1-methyl-alpha-D-glucopyranosideEscherichia coli-pH 7.5, 37°C, mannose-specific enzyme in presence of 3 mM ferricyanide641864 2D-image
0.009-Methyl-alpha-D-glucosideEscherichia coli-wild-type enzyme641888 2D-image
0.5-o-nitrophenyl-beta-D-galactopyranosideStaphylococcus aureus-pH 7.5, IICBLac641889 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.15-2-(N-dansyl)aminoethyl-beta-D-thiogalactosideStaphylococcus aureus-pH 7.5, isoenzyme IICBLac641889 2D-image
0.62-5-thioglucoseEnterococcus faecalis-25°C641872 2D-image
0.009-alpha-D-gluco-hexodialdo-1,5-pyranosideEscherichia coli-pH 7.5641885 2D-image
0.003-D-gluco-hexodialdo-1,5-pyranoseEscherichia coli-pH 7.5641885 2D-image
0.011-isopropyl-beta-D-thiogalactosideStaphylococcus aureus-pH 7.5, isoenzyme IICBLac641889 2D-image
0.1-MannoseEnterococcus faecalis-25°C641872 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1.77-Salmonella enterica subsp. enterica serovar Typhimurium--641869
4.52-Staphylococcus aureus-IICBlac641889
5.3-Escherichia coli--641875
10.1-Escherichia coli--641862
52-Staphylococcus aureus-the value corrected for enzyme II decay is 110641871
additional information-Escherichia coli-2 assay systems: assay I measuring the phosphoenolpyruvate-dependent phosphorylation of sugar in presence of the enzymes of the phosphotransferase system; assay II measuring the transphosphorylation from sugar to sugar in presence of EC 2.7.1.69 alone641865
additional information-Salmonella enterica subsp. enterica serovar Typhimurium-2 assay systems: assay I measuring the phosphoenolpyruvate-dependent phosphorylation of sugar in presence of the enzymes of the phosphotransferase system641870

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6-Escherichia coli-enzyme reconstituted in phospholipid vesicles; mannitol-dependent transphosphorylation641867
6-Escherichia coli-mannitol-dependent transphosphorylation641874
6.5-Escherichia coli-mannitol-dependent transphosphorylation, phosphoenolpyruvate-dependent transphosphorylation, 2 optima: pH 6.5 and pH 8.5641866
7-Escherichia coli-mannitol-dependent transphosphorylation, phosphoenolpyruvate-dependent transphosphorylation, two optima: pH7.0 and pH 9.0641875
7.5-Escherichia coli-exchange reaction in which a phosphoryl moiety is transferred from one molecule of the heat stable phosphocarrier protein Hpr to another641863
8.5-Escherichia coli-phosphoenolpyruvate-dependent transphosphorylation, 2 optima: pH 6.5 and pH 8.5641866
9-Escherichia coli-phosphoenolpyruvate-dependent transphosphorylation, two optima: pH 7.0 and pH 9.0641875
9.5-Escherichia coli-phosphoenolpyruvate-dependent transphosphorylation641874

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.29.2Escherichia coli-less than 50% of maximal activity above pH 9.2 and below pH 5.2, phosphoenolpyruvate-dependent transphosphorylation641866
5.59Escherichia coli-pH 5.5: about 50% of maximal activity, pH 9.0: about 65% of maximal activity, mannitol-dependent reaction641867
67.5Escherichia coli-less than 50% of maximal activity above pH 7.5 and below pH 6, mannitol-dependent transphosphorylation641866
69Escherichia coli-pH 6.0: about 85% of maximal activity, pH 9.0: about 65% of maximal activity, exchange reaction in which a phosphoryl moiety is transferred from one molecule of the heat stable phosphocarrier protein Hpr to another641863

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.74-Mycoplasma capricolum-calculated from analysis of the presumptive translation product641882
6-Escherichia coli--641874

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
epithelial cellRattus norvegicus--671780Manually annotated by BRENDA team
erythrocyteRattus norvegicus--671780Manually annotated by BRENDA team
oocyteRattus norvegicus--671780Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolLactobacillus casei--5829675497Manually annotated by BRENDA team
membraneEscherichia coli--16020641861, 641862, 641864, 641875Manually annotated by BRENDA team
membraneEscherichia coli-a considerable portion of its polypeptide chain must also extend into a hydrophilic environment, presumably to cytoplasm; integral membrane protein16020641866Manually annotated by BRENDA team
membraneEscherichia coli-the NH2-terminal half of the enzyme resides within the membrane16020641868Manually annotated by BRENDA team
membraneSalmonella enterica subsp. enterica serovar Typhimurium--16020641869, 641870Manually annotated by BRENDA team
membraneStaphylococcus aureus--16020641871Manually annotated by BRENDA team
membraneEnterococcus faecalis--16020641872Manually annotated by BRENDA team
membraneEscherichia coli-integral membrane protein16020641874Manually annotated by BRENDA team
membraneEscherichia coli-enzymes II of the phosphotransferase system exist in two physically distinct forms, one tightly integrated into the membrane and one either soluble or loosely associated with the membrane16020641881Manually annotated by BRENDA team
membraneLactobacillus casei--16020675497Manually annotated by BRENDA team
solubleEscherichia coli-enzymes II of the phosphotransferase system exist in two physically distinct forms, one tightly integrated into the membrane and one either soluble or loosely associated with the membrane-641881Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3qnq, downloadSCOP (3qnq)CATH (3qnq)Bacillus cereus (strain ATCC 10987)
1ax3, downloadSCOP (1ax3)CATH (1ax3)Bacillus subtilis (strain 168)
1ble, downloadSCOP (1ble)CATH (1ble)Bacillus subtilis (strain 168)
1gpr, downloadSCOP (1gpr)CATH (1gpr)Bacillus subtilis (strain 168)
2l2q, downloadSCOP (2l2q)CATH (2l2q)Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
2wy2, downloadSCOP (2wy2)CATH (2wy2)Escherichia coli
1a3a, downloadSCOP (1a3a)CATH (1a3a)Escherichia coli (strain K12)
1a6j, downloadSCOP (1a6j)CATH (1a6j)Escherichia coli (strain K12)
1e2b, downloadSCOP (1e2b)CATH (1e2b)Escherichia coli (strain K12)
1f3z, downloadSCOP (1f3z)CATH (1f3z)Escherichia coli (strain K12)
1ggr, downloadSCOP (1ggr)CATH (1ggr)Escherichia coli (strain K12)
1gla, downloadSCOP (1gla)CATH (1gla)Escherichia coli (strain K12)
1glb, downloadSCOP (1glb)CATH (1glb)Escherichia coli (strain K12)
1glc, downloadSCOP (1glc)CATH (1glc)Escherichia coli (strain K12)
1gld, downloadSCOP (1gld)CATH (1gld)Escherichia coli (strain K12)
1gle, downloadSCOP (1gle)CATH (1gle)Escherichia coli (strain K12)
1h9c, downloadSCOP (1h9c)CATH (1h9c)Escherichia coli (strain K12)
1iba, downloadSCOP (1iba)CATH (1iba)Escherichia coli (strain K12)
1iib, downloadSCOP (1iib)CATH (1iib)Escherichia coli (strain K12)
1o2f, downloadSCOP (1o2f)CATH (1o2f)Escherichia coli (strain K12)
1o53, downloadSCOP (1o53)CATH (1o53)Escherichia coli (strain K12)
1pdo, downloadSCOP (1pdo)CATH (1pdo)Escherichia coli (strain K12)
1vrc, downloadSCOP (1vrc)CATH (1vrc)Escherichia coli (strain K12)
1vsq, downloadSCOP (1vsq)CATH (1vsq)Escherichia coli (strain K12)
1wcr, downloadSCOP (1wcr)CATH (1wcr)Escherichia coli (strain K12)
2f3g, downloadSCOP (2f3g)CATH (2f3g)Escherichia coli (strain K12)
2few, downloadSCOP (2few)CATH (2few)Escherichia coli (strain K12)
2jzh, downloadSCOP (2jzh)CATH (2jzh)Escherichia coli (strain K12)
2jzn, downloadSCOP (2jzn)CATH (2jzn)Escherichia coli (strain K12)
2jzo, downloadSCOP (2jzo)CATH (2jzo)Escherichia coli (strain K12)
2kyr, downloadSCOP (2kyr)CATH (2kyr)Escherichia coli (strain K12)
2wwv, downloadSCOP (2wwv)CATH (2wwv)Escherichia coli (strain K12)
3bp3, downloadSCOP (3bp3)CATH (3bp3)Escherichia coli (strain K12)
1h9c, downloadSCOP (1h9c)CATH (1h9c)Escherichia coli O157:H7
1tvm, downloadSCOP (1tvm)CATH (1tvm)Escherichia coli O157:H7
1wcr, downloadSCOP (1wcr)CATH (1wcr)Escherichia coli O157:H7
3eye, downloadSCOP (3eye)CATH (3eye)Escherichia coli O157:H7
1h9c, downloadSCOP (1h9c)CATH (1h9c)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
1o53, downloadSCOP (1o53)CATH (1o53)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
1tvm, downloadSCOP (1tvm)CATH (1tvm)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
1wcr, downloadSCOP (1wcr)CATH (1wcr)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
1nrz, downloadSCOP (1nrz)CATH (1nrz)Klebsiella pneumoniae
1e2a, downloadSCOP (1e2a)CATH (1e2a)Lactococcus lactis subsp. lactis
2e2a, downloadSCOP (2e2a)CATH (2e2a)Lactococcus lactis subsp. lactis
2gpr, downloadSCOP (2gpr)CATH (2gpr)Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
2a0j, downloadSCOP (2a0j)CATH (2a0j)Neisseria meningitidis serogroup B (strain MC58)
1o53, downloadSCOP (1o53)CATH (1o53)Shigella flexneri
1tvm, downloadSCOP (1tvm)CATH (1tvm)Shigella flexneri
1wcr, downloadSCOP (1wcr)CATH (1wcr)Shigella flexneri
3bjv, downloadSCOP (3bjv)CATH (3bjv)Streptococcus mutans
3czc, downloadSCOP (3czc)CATH (3czc)Streptococcus mutans
3l8r, downloadSCOP (3l8r)CATH (3l8r)Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
3p3v, downloadSCOP (3p3v)CATH (3p3v)Streptococcus pyogenes serotype M1
3kv1, downloadSCOP (3kv1)CATH (3kv1)Vibrio fischeri (strain ATCC 700601 / ES114)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
16700-Mycoplasma capricolum-analytical ultracentrifugation641882
18130-Escherichia coli-mass spectrometry641887
105000-Salmonella enterica subsp. enterica serovar Typhimurium-analytical ultracentrifugation641869
400000-Staphylococcus aureus-gel filtration641871
additional information-Escherichia coli-enzyme elutes in two peaks corresponding to monomer and oligomer, gel filtration692907

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Escherichia coli-x * 68356, N-acetylglucosamine-specific enzyme, calculation from nucleotide sequence of cDNA641861
?Escherichia coli-x * 60000, SDS-PAGE641866, 641874, 641875
?Escherichia coli-x * 67893, mannitol-specific enzyme, calculation from nucleotide sequence of cDNA641868
?Salmonella enterica subsp. enterica serovar Typhimurium-x * 40000, SDS-PAGE641869
?Staphylococcus aureus-x * 55000, SDS-PAGE, gel filtration of SDS-treated enzyme641871
oligomerEscherichia coli-and monomer, x * 94000, fusion-protein of integral membrane subunit IICBGlc and malotose-binding protein, SDS-PAGe and calculated692907
monomerEscherichia coli-and oligomer, 1 * 94000, fusion-protein of integral membrane subunit IICBGlc and malotose-binding protein, SDS-PAGe and calculated692907
additional informationBacillus sp., Clostridium sp.-except Escherichia coli IIman all EII species consist of a single polypeptide chain but higher molecular weight complexes have been observed in Salmonella typhimurium IIglc, Escherichia coli IImtl and IIman641860
additional informationEscherichia coli-enzyme IImtl is cross-linked to a dimer through an activity-linked thiol using bifunctional maleimides and oxidizing agents. Enzyme IIman which consists of two polypeptide chains totaling 59000 Da has an apparent molecular mass of 240000 Da upon gel filtration, suggesting a higher molecular weight complex; except Escherichia coli IIman all EII species consist of a single polypeptide chain but higher molecular weight complexes have been observed in Salmonella typhimurium IIglc, Escherichia coli IImtl and IIman641860
additional informationKlebsiella sp., Lactobacillus sp., Mycoplasma sp.-except Escherichia coli IIman all EII species consist of a single polypeptide chain but higher molecular weight complexes have been observed in Salmonella typhimurium IIglc, Escherichia coli IImtl and IIman641860
additional informationSalmonella enterica subsp. enterica serovar Typhimurium-enzyme IIglc appears as a dimer during gel filtration and analytical ultracentrifugation; except Escherichia coli IIman all EII species consist of a single polypeptide chain but higher molecular weight complexes have been observed in Salmonella typhimurium IIglc, Escherichia coli IImtl and IIman641860
additional informationStaphylococcus aureus, Streptococcus sp.-except Escherichia coli IIman all EII species consist of a single polypeptide chain but higher molecular weight complexes have been observed in Salmonella typhimurium IIglc, Escherichia coli IImtl and IIman641860
additional informationEscherichia coli-Enzyme IIGlc is active as a monomer. A dimeric form is detected by chemical cross-linking and by zonal sedimentation at 4°C. Upon mild oxidation a disulfide bond is formed between the subunits of the dimer. Oxidized IIGlc is more stable than the reduced form, but is inactive because it cannot be phosphorylated by the cytoplasmic subunit IIGlc of the glucose permease641862
additional informationEscherichia coli-at high concentrations the enzyme exists in an aggregated or oligomeric state, this form is more active than the monomeric or dissociated form of the enzyme in catalyzing the vectorial mannitol transphosphorylation641868
additional informationSalmonella enterica subsp. enterica serovar Typhimurium-the solubilized enzyme exists as a complex of MW 105000 Da641869
additional informationEscherichia coli-the membrane-integrated enzymes II are largely dimeric, whereas the soluble enzymes II are largely monomeric641881

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
crystals are obtained in 57-62% saturated ammonium sulfate solution, 0.5% w/vBacillus subtilis-641859
hanging-drop vapor diffusion method, IIA domainBacillus subtilis-641857
IIB subunit of fructoase permeaseBacillus subtilis-641880
hanging-drop vapor diffusion method, IIA domainEscherichia coli-641858
mannitol-specific IIA domainEscherichia coli-641879
crystal structure of the IIBSor domain of the sorbose permease solved to 1.75 A resolutionKlebsiella pneumoniae-641878

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
additional information-Mycoplasma capricolum-the enzyme undergoes reversible, two-state thermal unfolding with Tm: 70°C641882

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
repeated freezing and thawing does not affect the phosphorylation activity but freezing can alter the physical propertiesEscherichia coli-641862
stabilization of IIBLac-His for several weeks is achieved in 50% glycerol and by storage at -20°CStaphylococcus aureus-641889

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-70°CEscherichia coli-641865, 641866
-70°C, long-term storage in 25 mM sodium phosphate buffer, pH 7.0, 1% polydisperse octyl-oligooxyethylene, 1 mM EDTA, 10% glycerol, short-term storage is possible without glycerolEscherichia coli-641862
-70°C, stable for at least 2 monthsEscherichia coli-641875
4°C, stable for several daysEscherichia coli-641875
-70°C, several weeksSalmonella enterica subsp. enterica serovar Typhimurium-641869
4°C, 1 weekSalmonella enterica subsp. enterica serovar Typhimurium-641869

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Enterococcus faecalis-641872
-Escherichia coli-641866, 641875
enzymatically active C-terminal domain of enzyme IImtlEscherichia coli-641877
fusion-protein of integral membrane subunit IICBGlc and malotose-binding protein. Fusion protein is fully active and exhibits all of the catalytic properties of the native enzymeEscherichia coli-692907
IImtlEscherichia coli-641865
membrane subunit IIGlc purified from overproducing Escherichia coliEscherichia coli-641862
recombinant enzyme IIAglcMycoplasma capricolum-641882
-Salmonella enterica subsp. enterica serovar Typhimurium-641869
isoenzyme IIlacStaphylococcus aureus-641871

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-641868
BglF derivative in which the order of the domains is CBAEscherichia coli-641886
enzymatically active C-terminal domain of enzyme IImtlEscherichia coli-641877
enzyme IIN-acetylglucosamineEscherichia coli-641861
fusion of integral membrane subunit IICBGlc encoded by ptsG, with maltose-binding proteinEscherichia coli-692907
gene ptsIEscherichia coli-692830
subcloning and expression of the three individual domains IIAbgl, IIBbgl and IICbgl, as well as truncated BglF proteins which lack one domainEscherichia coli-641883
expressed in Escherichia coli strain LJ140Mycobacterium smegmatis-705222
cloned into a regulated expression vector, expression in Escherichia coliMycoplasma capricolum-641882
expressed in Saccharomyces cerevisiae strain HD300Rattus norvegicus-671780
construction of a recombinant IICBLac with a C-terminal with a C-terminal affinity tag of six His residues and of a singly IIBlac-His protein, expression in Escherichia coliStaphylococcus aureus-641889

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C461DBacillus subtilis-Cys461 and His620 are required for the function of the enzyme. A replacement of these residues results in loss of glucose repression of bglPH operon expression and beta-xylosidase synthesis641873
H620DBacillus subtilis-Cys461 and His620 are required for the function of the enzyme. A replacement of these residues results in loss of glucose repression of bglPH operon expression and beta-xylosidase synthesis641873
G320VEscherichia coli-G320V-EIIGlc, mutation results in a G320 to V substitution that allows EIIGlc to transport mannitol641888
H90DEscherichia coli-H90DE-EIIAGlc does not undergo phosphorylation to create an unstable phosphoacyl but possibly forms an abortive complex with the other PTS proteins limiting their phosphorylation641887
additional informationEscherichia coli-BglF derivative IICBAbgl, in which the order of the domains is different from the wild-type enzyme, behaves like wild-type enzyme in its ability to be phosphorylated and to phosphorylate BglG in vitro and in vivo. However, it can not catalyze phosphorylation of beta-glucosides in vitro nor their phosphorylation in vivo and can not catalyze BglG dephosphorylation in vitro and in vivo641886
additional informationEscherichia coli-replacement of HPr and EI of Escherichia coli with the homologous proteins from Bacillus subtilis, a gram-positive bacterium, leads to severe growth defects on PTS sugars, suggesting that HPr of Bacillus subtilis cannot efficiently phosphorylate the EIIs of Escherichia coli, enhanced phosphorylation is achieved with Bacillus subtilis HPr mutants, overview692830
additional informationEscherichia coli-fusion of integral membrane subunit IICBGlc encoded by ptsG, with maltose-binding protein692907

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
reconstitution of mannitol-dependent mannitol transphosphorylationEscherichia coli-641867

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
641857Kapadia, G.; Chen, C.C.H.; Reddy, P.; Saier, M.H.; Reizer, J.; Herzberg, O.Crystallization of the IIA domain of the glucose permease of Bacillus subtilisJ. Mol. Biol.2211079-10801991Bacillus subtilis PubMed
641858Lammers, L.A.; Dijkstra, B.W.; van Weeghel, R.P.; Pas, H.H.; Robillard, G.T.Crystallization of the A-domain of the mannitol transport protein enzyme IImtlJ. Mol. Biol.228310-3121992Escherichia coli PubMed
641859Liao, D.I.; Kapadia, G.; Reddy, P.; Saier, M.H.; Reizer, J.; Herzberg, O.Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolutionBiochemistry309583-95941991Bacillus subtilis PubMed
641860Robillard, G.T.; Lolkema, J.S.Enzymes II of the phosphoenolpyruvate-dependent sugar transport systems: a review of their structure and mechanism of sugar transportBiochim. Biophys. Acta947493-5191988Bacillus sp., Clostridium sp., Escherichia coli, Klebsiella sp., Lactobacillus sp., Mycoplasma sp., Salmonella enterica subsp. enterica serovar Typhimurium, Staphylococcus aureus, Streptococcus sp. PubMed
641861Peri, K.G.; Waygood, E.B.Sequence of cloned enzyme IIN-acetylglucosamine of the phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of Escherichia coliBiochemistry276054-60611988Escherichia coli PubMed
641862Meins, M.; Zanolari, B.; Rosenbusch, J.P.; Erni, B.Glucose permease of Escherichia coli. Purification of the IIGlc subunit and functional characterization of its oligomeric formsJ. Biol. Chem.26312986-129931988Escherichia coli PubMed
641863Sutrina, S.L.; Waygood, E.B.; Grenier, F.C.; Saier, M.H.HPr/HPr-P phosphoryl exchange reaction catalyzed by the mannitol specific enzyme II of the bacterial phosphotransferase systemJ. Biol. Chem.2622636-26411987Escherichia coli PubMed
641864Grenier, F.C.; Waygood, E.B.; Saier, M.H.Bacterial phosphotransferase system: regulation of the glucose and mannose enzymes II by sulfhydryl oxidationBiochemistry244872-48761985Escherichia coli PubMed
641865Grenier, F.C.; Waygood, E.B.; Saier, M.H.Bacterial phosphotransferase system: regulation of mannitol enzyme II activity by sulfhydryl oxidationBiochemistry2447-511985Escherichia coli PubMed
641866Jacobson, G.R.; Lee, C.A.; Leonard, J.E.; Saier, M.H.Mannitol-specific enzyme II of the bacterial phosphotransferase system. I. Properties of the purified permeaseJ. Biol. Chem.25810748-107561983Escherichia coli PubMed
641867Leonard, J.E.; Saier, M.H.Mannitol-specific enzyme II of the bacterial phosphotransferase system. II. Reconstitution of vectorial transphosphorylation in phospholipid vesiclesJ. Biol. Chem.25810757-107601983Escherichia coli PubMed
641868Lee, C.A.; Saier, M.H.Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease geneJ. Biol. Chem.25810761-107671983Escherichia coli PubMed
641869Erni, B.; Trachsel, H.; Postma, P.W.; Rosenbusch, J.P.Bacterial phosphotransferase system. Solubilization and purification of the glucose-specific enzyme II from membranes of Salmonella typhimuriumJ. Biol. Chem.25713726-137301982Salmonella enterica subsp. enterica serovar Typhimurium PubMed
641870Waygood, E.B.; Meadow, N.D.Assays for the phosphotransferase system from Salmonella typhimuriumMethods Enzymol.90423-4311982Salmonella enterica subsp. enterica serovar Typhimurium-
641871Schäfer, A.; Schrecker, O.; Hengstenberg, W.The staphylococcal phosphoenolpyruvate-dependent phosphotransferase system. Purification and characterisation of the galactoside-specific membrane-component enzyme IIEur. J. Biochem.113289-2941981Staphylococcus aureus PubMed
641872Hüdig, H.; Hengstenberg, W.The bacterial phosphoenolpyruvate dependent phosphotransferase system (PTS): solubilisation and kinetic parameters of the glucose-specific membrane bound enzyme II component of Streptococcus faecalisFEBS Lett.114103-1061980Enterococcus faecalis PubMed
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641874Saier, M.H.Catalytic activities associated with the enzymes II of the bacterial phosphotransferase systemJ. Supramol. Struct.14281-2941980Escherichia coli PubMed
641875Jacobson, G.R.; Lee, C.A.; Saier, M.H.Purification of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase systemJ. Biol. Chem.254249-2521979Escherichia coli PubMed
641876Sussman, M.L.; Hays, J.B.; Smith, T.A.G.Selective, reversible inhibition of the lactose phosphotransferase system of Staphylococcus aureus by dodecyl sulfate and deoxycholateArch. Biochem. Biophys.182134-1371977Staphylococcus aureus PubMed
641877van Weeghel, R.P.; Meyer, G.H.; Keck, W.; Robillard, G.T.Phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli: overexpression, purification, and characterization of the enzymatically active C-terminal domain of enzyme IImtl equivalent to enzyme IIImtlBiochemistry301774-17791991Escherichia coli PubMed
641878Orriss, G.L.; Erni, B.; Schirmer, T.Crystal structure of the IIBSor domain of the sorbose permease from Klebsiella pneumoniae solved to 1.75 A resolutionJ. Mol. Biol.3271111-11192003Klebsiella pneumoniae PubMed
641879Van Montfort, R.L.M.; Pijning, T.; Kalk, K.H.; Hangyi, I.; Kouwijzer, M.L.C.E.; Robillard, G.T.; Dijkstra, B.W.The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active siteStructure6377-3881998Escherichia coli PubMed
641880Schauder, S.; Nunn, R.S.; Lanz, R.; Erni, B.; Schirmer, T.Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilisJ. Mol. Biol.276591-6021998Bacillus subtilis PubMed
641881Aboulwafa, M.; Saier, M.H., Jr.Soluble sugar permeases of the phosphotransferase system in Escherichia coli: Evidence for two physically distinct forms of the proteins in vivoMol. Microbiol.48131-1412003Escherichia coli PubMed
641882Zhu, P.P.; Nosworthy, N.; Ginsburg, A.; Miyata, M.; Seok, Y.J.; Peterkofsky, A.Expression, purification, and characterization of enzyme IIAglc of the phosphoenolpyruvate:sugar phosphotransferase system of Mycoplasma capricolumBiochemistry366947-69531997Mycoplasma capricolum PubMed
641883Chen, Q.; Amster-Choder, O.BglF, the Escherichia coli beta-glucoside permease and sensor of the bgl system: domain requirements of the different catalytic activitiesJ. Bacteriol.181462-4681999Escherichia coli PubMed
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641889Peters, D.; Frank, R.; Hengstenberg, W.Lactose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. Purification of the histidine-tagged transmembrane component IICBLac and its hydrophilic IIB domain by metal-affinity chromatography, and functional characterizationEur. J. Biochem.228798-8041995Staphylococcus aureus PubMed
661794Moon, M.W.; Kim, H.J.; Oh, T.K.; Shin, C.S.; Lee, J.S.; Kim, S.J.; Lee, J.K.Analyses of enzyme II gene mutants for sugar transport and heterologous expression of fructokinase gene in Corynebacterium glutamicum ATCC 13032FEMS Microbiol. Lett.244259-2662005Corynebacterium glutamicum PubMed
671496Maze, A.; OConnell-Motherway, M.; Fitzgerald, G.F.; Deutscher, J.; van Sinderen, D.Identification and characterization of a fructose phosphotransferase system in Bifidobacterium breve UCC2003Appl. Environ. Microbiol.73545-5532007Bifidobacterium breve PubMed
671780Liu, Z.; Sanchez, M.A.; Jiang, X.; Boles, E.; Landfear, S.M.; Rosen, B.P.Mammalian glucose permease GLUT1 facilitates transport of arsenic trioxide and methylarsonous acidBiochem. Biophys. Res. Commun.351424-4302006Rattus norvegicus PubMed
673756Baruffini, E.; Goffrini, P.; Donnini, C.; Lodi, T.Galactose transport in Kluyveromyces lactis: major role of the glucose permease Hgt1FEMS Yeast Res.61235-12422006Kluyveromyces lactis PubMed
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675849Yebra, M.J.; Monedero, V.; Zuniga, M.; Deutscher, J.; Perez-Martinez, G.Molecular analysis of the glucose-specific phosphoenolpyruvate:sugar phosphotransferase system from Lactobacillus casei and its links with the control of sugar metabolismMicrobiology15295-1042006Lactobacillus casei PubMed
692830Reichenbach, B.; Breustedt, D.A.; Stuelke, J.; Rak, B.; Goerke, B.Genetic dissection of specificity determinants in the interaction of HPr with enzymes II of the bacterial phosphoenolpyruvate:sugar phosphotransferase system in Escherichia coliJ. Bacteriol.1894603-46132007Escherichia coli PubMed
692907Aboulwafa, M.; Saier, M.H.Characterization of the E. coli glucose permease fused to the maltose-binding proteinJ. Basic Microbiol.483-92008Escherichia coli PubMed
705222Pimentel-Schmitt, E.F.; Jahreis, K.; Eddy, M.P.; Amon, J.; Burkovski, A.; Titgemeyer, F.Identification of a glucose permease from Mycobacterium smegmatis mc2 155J. Mol. Microbiol. Biotechnol.16169-1752009Mycobacterium smegmatis PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.69)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)