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Information on EC 2.7.3.9 - phosphoenolpyruvate-protein phosphotransferase and Organism(s) Escherichia coli and UniProt Accession P08839
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2.7.3.9 phosphoenolpyruvate-protein phosphotransferaseIUBMB Comments
Enzyme I of the phosphotransferase system (cf. EC 2.7.1.69 protein-Npi-phosphohistidine---sugar phosphotransferase). Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. A similar reaction, where the protein is the enzyme EC 2.7.9.2 pyruvate, water dikinase, is part of the mechanism of that enzyme.
Specify your search results
Word Map
- 2.7.3.9
- hpr
-
phosphocarrier
- fructose
-
permease
- streptococcus
-
catabolite
-
histidine-containing
- typhimurium
- mannitol
- lactose
-
glucose-specific
-
non-pts
-
iiiglc
-
antiterminator
-
unphosphorylated
- mutans
-
mannitol-specific
-
histidyl
- cellobiose
- 2-deoxyglucose
-
alpha-glucoside
- casei
- salivarius
- melibiose
-
energy-coupling
-
beta-glucoside
-
pep-dependent
-
fructose-specific
-
eiias
- medicine
-
starch-branching
- glucitol
- drug development
-
nonmetabolizable
- dikinase
-
transphosphorylation
- carnosus
- capricolum
-
hexitols
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
enzyme i, phosphoenolpyruvate:sugar phosphotransferase system, phosphoenolpyruvate-dependent phosphotransferase system, phosphoenolpyruvate:carbohydrate phosphotransferase system, phosphoenolpyruvate:glycose phosphotransferase system, phosphoenolpyruvate-dependent phosphotransferase, phosphoenolpyruvate:sugar phosphotransferase, enzyme i of the phosphotransferase system, phosphoenolpyruvate-protein phosphotransferase, phosphotransferase enzyme i, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
-
enzyme I of the phosphotransferase system
-
-
-
-
phosphoenolpyruvate sugar phosphotransferase enzyme I
-
-
-
-
phosphopyruvate-protein factor phosphotransferase
-
-
-
-
phosphopyruvate-protein phosphotransferase
-
-
-
-
phosphotransferase system enzyme I
-
-
-
-
phosphotransferase, phosphoenolpyruvate-protein
-
-
-
-
sugar-PEP phosphotransferase enzyme I
-
-
-
-
additional information
additional information
-
enzyme I is part of the phosphoenolpyruvate-carbohydrate phosphotransferase system
additional information
-
enzyme I is part of the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
bi-bi ping-pong mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:protein-L-histidine Npi-phosphotransferase
Enzyme I of the phosphotransferase system (cf. EC 2.7.1.69 protein-Npi-phosphohistidine---sugar phosphotransferase). Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. A similar reaction, where the protein is the enzyme EC 2.7.9.2 pyruvate, water dikinase, is part of the mechanism of that enzyme.
CAS REGISTRY NUMBER
COMMENTARY
37278-17-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
-
-
-
-
r
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
-
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
the phosphoryl group is transferred from phosphoenolpyruvate to the enzyme and to a low molecular weight phosphocarrier protein, phosphorylation rate of the enzyme increases at presence of the phosphorylated phosphocarrier protein, phosphoryl group transfer proceeds in 4 reactions
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
r
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
in a first reaction step phosphate is transferred to the N-3 position of the imidazole ring of histidine
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
the enzyme is essential for the catabolism of many sugars by bacterial cells
-
-
?
phosphoenolpyruvate + HPr
pyruvate + phospho-HPr
-
the first two reactions in the phosphotransfer sequence of bacterial phosphoenolpyruvate:glycose phosphotransferase systems are the autophosphorylation of enzyme I by phosphoenolpyruvate followed by the transfer of the phospho group to the low-molecular weight protein, HPr
-
-
r
phosphoenolpyruvate + HPr
pyruvate + phospho-HPr
-
the dimer of enzyme I, EI2, can phosphorylate multiple molecules of HPr without dissociating to a monomer. The monomer of enzyme I, EI, can accept a phospho group from phospho-HPr
-
-
r
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
r
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
enzyme I catalyzes two reversible reactions: an Mg2+-dependent autophosphorylation reaction using phosphoenolpyruvate as a substrate, and a phosphotransfer reaction to histidine-containing phosphocarrier protein
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
the enzyme is essential for the catabolism of many sugars by bacterial cells
-
-
?
phosphoenolpyruvate + HPr
pyruvate + phospho-HPr
-
the first two reactions in the phosphotransfer sequence of bacterial phosphoenolpyruvate:glycose phosphotransferase systems are the autophosphorylation of enzyme I by phosphoenolpyruvate followed by the transfer of the phospho group to the low-molecular weight protein, HPr
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
Mg2+
induces small conformational changes, large conformational changes with Mg2+ and phosphoenolpyruvate, swivelling mechanism, dimerization of the enzyme depends on its ligands
Mg2+
-
necessary for dimerization, only the dimeric enzyme can be phosphorylated
Mg2+
-
enzyme I of the PEP:sugar phosphotransferase system is regulated by a monomer-dimer equilibrium. A Mg2+-dependent autophosphorylation by phosphoenolpyruvate requires the homodimer. Physiological concentrations of phosphoenolpyruvate and Mg2+ increase, whereas pyruvate and Mg2+ decrease the amount of dimeric, active dephospho-enzyme I
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,7-diacetyl-6-(5-carboxy-6,7-dihydroxy-4-oxochromen-3-yl)-2,3-dihydroxy-9-oxoxanthene-1-carboxylic acid
-
-
methyl 2-((3-[(1-methoxy-1-oxopropan-2-yl)oxy]-9-oxo-9H-xanthen-1-yl)oxy)propanoate
-
-
propan-2-yl,2-((9-oxo-3-[2-oxo-2-(propan-2-yloxy)ethoxy]-9H-xanthen-1-yl)oxy)acetate
-
-
pyruvate
-
physiological concentrations of pyruvate and Mg2+ decrease the amount of dimeric, active dephospho-enzyme I
additional information
-
not inhibitory: AMP, ADP, ATP, GMP, GDP, GTP, cAMP, cGMP, acetyl-CoA, acetyl phosphate, glucose 6-phosphate, glucose 1-phosphate, fructose 1,6-diphosphate, L-histidine, D-histidine
-
additional information
-
enzyme-inhibitor molecular docking of the ligand molecule, xanthone derivative ZINC14764604 or (4,5,6-triacetyloxy-9-oxoxanthen-3-yl)acetate, with the EI-HPr (histidine-containing phosphoryl carrier protein) complex, PDB ID 3EZA, and structure modelling, overview. Residues His189 of EI and His15 of HPr are involved in binding
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphoenolpyruvate
-
physiological concentrations of phosphoenolpyruvate and Mg2+ increase the amount of dimeric, active dephospho-enzyme I
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme in cells from dense colonies grown on agar plates with LB medium or synthetic Neidhardt medium shows primarily bipolar or punctated distribution (concentrated in numerous discrete spots throughout the cell). In liquid culture, under carefully defined carbon-limiting growth conditions cellular levels of active enzyme remain constant for each carbon source, but distribution depends on C source, cell density, growth phase, and apparently on conditioned medium. Determination is diffuse (dispersed throughout the cell) during exponential growth on LB medium or ribose/Neidhardt medium. On ribose distribution is punctate in the stationary phase, reverting to diffuse when more ribose is added. In LB medium, both wild-type enzyme and a nonphosphorylatable mutant, H189Q, show a diffuse distribution during growth, but, shortly after the addition of isopropyl beta-D-thiogalactopyranoside distribution of wild-type enzyme becomes bipolar, trhat of H189Q-Y-EI does not
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the phosphoenolpyruvate phosphotransferase system (PTS) is ubiquitous in eubacteria and absent from eukaryotes
malfunction
-
deficiency of enzyme I, EI, of the phosphoenolpyruvate phosphotransferase system in bacterial mutants lead to severe growth defects
metabolism
physiological function
metabolism
-
all phosphotransferase system proteins inclusive enzyme I required to transport glucose in Escherichia coli regulate a metabolic function
metabolism
-
the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system constitutes a complex transport and sensory system and consists of two cytoplasmic energy-coupling proteins, Enzyme I (EI) and HPr, and one of more than 20 different carbohydrate-specific membrane proteins named Enzyme II (EII), which catalyze the uptake and concomitant phosphorylation of numerous carbohydrates
metabolism
-
the phosphoenolpyruvate phosphotransferase system consists of two phosphoryl carriers, enzyme I (EI) and the histidine-containing phosphoryl carrier protein (HPr), and several PTS transporters, catalyzing the concomitant uptake and phosphorylation of several carbohydrates
physiological function
-
the phosphoenolpyruvate-carbohydrate phosphotransferase system represents the most efficient system for the transport and phosphorylation of sugars, such as glucose
physiological function
-
the phosphorylation state of enzyme I of phosphoenolpyruvate phosphotransferase system is important for Lsr activation and AI-2 internalization
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
monomer or dimer
-
x * 63500, enzyme I, EI, the monomer undergoes a monomer/dimer transition and only the dimer form accepts the phosphoryl group from phosphoenolpyruvate. The crystal structure of EI, PDB ID 1ZYM, reveals a dimeric protein in which each subunit comprises three domains: a domain that binds the partner HPr, a domain that carries the phosphorylated histidine residue, and a PEP-binding domain
additional information
-
enzyme I of the PEP:sugar phosphotransferase system is regulated by a monomer-dimer equilibrium. A Mg2+-dependent autophosphorylation by phosphoenolpyruvate requires the homodimer. Physiological concentrations of phosphoenolpyruvate and Mg2+ increase, whereas pyruvate and Mg2+ decrease the amount of dimeric, active dephospho-enzyme I
dimer
homodimers accept phosphoryl group from phosphoenolpyruvate, monomer does not
dimer
only the dimer accepts the phoshphoryl group from phosphoenolpyruvate, the monomer consists of two major domains at the N- and C- termini, the C- terminal domain forms dimers before Mg2+, phosphoenolpyruvate and the N- terminal domain bind
dimer
-
dimerization is induced by phosphoenolpyruvate and Mg2+, dimer is the active form of enzyme
dimer
-
the enzyme is dimeric at room temperature and dissociates to a catalytically not active monomer at 4-6°C
dimer
-
enzyme exists in a monomer-dimer equilibrium, monomer-dimer association regulates activity
dimer
-
the dimer of enzyme I, EI2, can phosphorylate multiple molecules of HPr without dissociating to a monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the C-terminal domain can phosphorylate the N-terminal domain of enzyme I, but their binding is transient regardless of the presence of phosphoenolpyruvate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by vapour diffusion in hanging drops in presence of Mg2+, phosphoenolpyruvate and oxalate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G356S
the mutant shows reduced dimerization affinity and lower autophosphorylation activity compared to the wild type enzyme
H189A
H189E
additional information
additional information
-
fusion protein of enzyme plus the remaining three subunits of glucose phosphotransferase system and Ala-Pro-rich linker sequences
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM sodium phosphate buffer, pH 7.2, 1 mM NaN3, dithiothreitol, stable for months, but instable in Tris buffer
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column or HisTrap column chromatography, Superdex 75 gel filtration and MonoQ column chromatography
from overproducing transformants, also the N and C terminal domain of the enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
in overproducing transformants, also the N- and C- terminal domain of the enzyme were cloned and expressed separately
the C-terminal and N-terminal domains of enzyme I are expressed in Escherichia coli BL21star(DE3) cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
enzyme I, EI, of the phosphoenolpyruvate phosphotransferase system isa drug target to develop antimicrobial agents, xanthone derivatives have high potential to be developed as antibiotics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Napper, S.; Brokx, S.J.; Pally, E.; Kindrachuk, J.; Delbaere, L.T.J.; Waygood, E.B.
Substitution of aspartate and glutamate for active center histidines in the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system maintain phosphotransfer potential
J. Biol. Chem.
276
41588-41593
2001
Escherichia coli
Chauvin, F.; Brand, L.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy
J. Biol. Chem.
269
20270-20274
1994
Escherichia coli
Chauvin, F.; Brand, L.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer equilibrium by fluorescence anisotropy
J. Biol. Chem.
269
20263-20269
1994
Escherichia coli
Waygood, E.B.
Enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system has two sites of phosphorylation per dimer
Biochemistry
25
4085-4090
1986
Escherichia coli
Hoving, H.; Koning, J.H.; Robillard, G.T.
Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: role of divalent metals in the dimerization and phosphorylation of enzyme I
Biochemistry
21
3128-3136
1982
Escherichia coli
Waygood, E.B.; Steeves, T.
Enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some properties
Can. J. Biochem.
58
40-48
1980
Escherichia coli
Misset, O.; Brouwer, M.; Robillard, G.T.
Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Evidence that the dimer is the active form of enzyme I
Biochemistry
19
883-890
1980
Escherichia coli
Robillard, G.T.; Dooijewaard, G.; Lolkema, J.
Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. Complete purification of enzyme I by hydrophobic interaction chromatography
Biochemistry
18
2984-2989
1979
Escherichia coli
-
Postma, P.W.; Roseman, S.
The bacterial phosphoenolpyruvate: sugar phosphotransferase system
Biochim. Biophys. Acta
457
213-257
1976
Escherichia coli, Staphylococcus aureus, Salmonella enterica subsp. enterica serovar Typhimurium
Walsh, C.T.; Kabak, H.R.
Vinylglycolic acid. An inactivator of the phosphoenolpyruvate-phosphate transferase system in Escherichia coli
J. Biol. Chem.
248
5456-5462
1973
Escherichia coli
Saffen, D.W.; Presper, K.A.; Doering, T.L.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes
J. Biol. Chem.
262
16241-16253
1987
Escherichia coli
De Reuse, H.; Danchin, A.
The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription
J. Bacteriol.
170
3827-3837
1988
Escherichia coli
Chauvin, F.; Fomenkov, A.; Johnson, C.R.; Roseman, S.
The N-terminal domain of Escherichia coli enzyme I of the phosphoenolpyruvate/glycose phosphotransferase system: molecular cloning and characterization
Proc. Natl. Acad. Sci. USA
93
7028-7031
1996
Escherichia coli
Dimitrova, M.N.; Szczepanowski, R.H.; Ruvinov, S.B.; Peterkofsky, A.; Ginsburg, A.
Interdomain Interaction and Substrate Coupling Effects on Dimerization and Conformational Stability of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System
Biochemistry
41
906-913
2002
Escherichia coli
Ginsburg, A.; Szczepanowski, R.H.; Ruvinov, S.B.; Nosworthy, N.J.; Sondej, M.; Umland, T.C.; Peterkofsky, A.
Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effects
Protein Sci.
9
1085-1094
2000
Escherichia coli
Mao, Q.; Schunk, T.; Gerber, B.; Erni, B.
A string of enzymes, purification and characterization of a fusion protein comprising the four subunits of the glucose phosphotransferase system of Escherichia coli
J. Biol. Chem.
270
18295-18300
1995
Escherichia coli
Napper, S.; Delbaere, L.T.J.; Waygood, E.B.
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization
J. Biol. Chem.
274
21776-21782
1999
Escherichia coli
Seok, Y.J.; Lee, B.R.; Gazdar, C.; Svenson, I.; Yadla, N.; Peterkofsky, A.
Importance of the region around glycine-338 for the activity of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system
Biochemistry
35
236-242
1996
Escherichia coli
Meadow, N.D.; Mattoo, R.L.; Savtchenko, R.S.; Roseman, S.
Transient state kinetics of Enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system of Escherichia coli: equilibrium and second-order rate constants for the phospho transfer reactions with phosphoenolpyruvate and HPr
Biochemistry
44
12790-12796
2005
Escherichia coli
Patel, H.V.; Vyas, K.A.; Li, X.; Savtchenko, R.; Roseman, S.
Subcellular distribution of enzyme I of the Escherichia coli phosphoenolpyruvate:glycose phosphotransferase system depends on growth conditions
Proc. Natl. Acad. Sci. USA
101
17486-17491
2004
Escherichia coli
Dimitrova, M.N.; Peterkofsky, A.; Ginsburg, A.
Opposing effects of phosphoenolpyruvate and pyruvate with Mg(2+) on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli
Protein Sci.
12
2047-2056
2003
Escherichia coli
Patel, H.V.; Vyas, K.A.; Savtchenko, R.; Roseman, S.
The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransferase system
J. Biol. Chem.
281
17570-17578
2006
Escherichia coli (P08839), Escherichia coli
Patel, H.V.; Vyas, K.A.; Mattoo, R.L.; Southworth, M.; Perler, F.B.; Comb, D.; Roseman, S.
Properties of the C-terminal domain of enzyme I of the Escherichia coli phosphotransferase system
J. Biol. Chem.
281
17579-17587
2006
Escherichia coli (P08839), Escherichia coli
Teplyakov, A.; Lim, K.; Zhu, P.P.; Kapadia, G.; Chen, C.C.; Schwartz, J.; Howard, A.; Reddy, P.T.; Peterkofsky, A.; Herzberg, O.
Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein
Proc. Natl. Acad. Sci. USA
103
16218-16223
2006
Escherichia coli (P08839), Escherichia coli
Escalante, A.; Salinas Cervantes, A.; Gosset, G.; Bolívar, F.
Current knowledge of the Escherichia coli phosphoenolpyruvate-carbohydrate phosphotransferase system: peculiarities of regulation and impact on growth and product formation
Appl. Microbiol. Biotechnol.
94
1483-1494
2012
Escherichia coli
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
Lazazzera, B.
The phosphoenolpyruvate phosphotransferase system: As important for biofilm formation by Vibrio cholerae as it is for metabolism in Escherichia coli
J. Bacteriol.
192
4083-4085
2010
Escherichia coli, Vibrio cholerae serotype O1
Pereira, C.; Santos, A.; Bejerano-Sagie, M.; Correia, P.; Marques, J.; Xavier, K.
Phosphoenolpyruvate phosphotransferase system regulates detection and processing of the quorum sensing signal autoinducer-2
Mol. Microbiol.
84
93-104
2012
Escherichia coli
Yun, Y.; Suh, J.
Calorimetric and spectroscopic investigation of the interaction between the C-terminal domain of enzyme I and its ligands
Protein Sci.
21
1726-1733
2012
Escherichia coli
Huang, K.J.; Lin, S.H.; Lin, M.R.; Ku, H.; Szkaradek, N.; Marona, H.; Hsu, A.; Shiuan, D.
Xanthone derivatives could be potential antibiotics: virtual screening for the inhibitors of enzyme I of bacterial phosphoenolpyruvate-dependent phosphotransferase system
J. Antibiot.
66
453-458
2013
Escherichia coli
EXTERNAL LINKS (specific for EC-Number 2.7.3.9)
Transporter Classification Database (TCDB): 4.A.2.1.11, 4.A.2.1.10, 8.A.7.1.1, 8.A.7.1.4, 4.A.2.1.17, 4.A.1.1.15, 4.A.2.1.26, 8.A.7.1.3, 8.A.7.1.6, 8.A.7.1.5, 8.A.7.1.2
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