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Information on EC 2.7.3.9 - phosphoenolpyruvate-protein phosphotransferase
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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.
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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 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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EIC
EIN
enzyme I
enzyme I of the phosphotransferase system
PEP:sugar phosphotransferase system enzyme I
phosphoenolpyruvate sugar phosphotransferase enzyme I
-
-
-
-
phosphoenolpyruvate-dependent phosphotransferase system
phosphoenolpyruvate-dependent phosphotransferase system enzyme I
phosphoenolpyruvate-protein phosphotransferase
phosphoenolpyruvate:carbohydrate phosphotransferase system
phosphoenolpyruvate:glucose/mannose phosphotransferase system
-
enzyme I
phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
phosphoenolpyruvate:sugar phosphotransferase system
phosphopyruvate-protein factor phosphotransferase
-
-
-
-
phosphopyruvate-protein phosphotransferase
-
-
-
-
phosphotransferase enzyme I
phosphotransferase system component enzyme I
phosphotransferase system enzyme I
phosphotransferase, phosphoenolpyruvate-protein
-
-
-
-
protein kinase enzyme I
PTS
ptsA
ptsI
sugar-PEP phosphotransferase enzyme I
-
-
-
-
YpqE
additional information
EIC
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
C-terminal domain of enzyme I
-
enzyme I of the phosphotransferase system
-
-
-
-
PEP:sugar phosphotransferase system enzyme I
-
-
phosphoenolpyruvate-dependent phosphotransferase system enzyme I
-
-
phosphoenolpyruvate-dependent phosphotransferase system enzyme I
-
-
-
phosphoenolpyruvate:carbohydrate phosphotransferase system
-
-
phosphoenolpyruvate:carbohydrate phosphotransferase system
-
-
-
phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
-
phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
-
phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
-
phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
-
phosphoenolpyruvate:sugar phosphotransferase system
-
phosphotransferase system enzyme I
-
-
-
-
ptsA
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
-
additional information
enzyme I is part of the phosphoenolpyruvate: sugar phosphotransferase system
additional information
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
enzyme I is part of the phosphoenolpyruvate: sugar phosphotransferase system
-
additional information
enzyme II is part of the bacterial phosphoenolpyruvate:sugar phosphotransferase system in Escherichia coli
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
additional information
the enzyme is part of the phosphoenolpyruvate:sugar phosphotransferase system
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + protein histidine = pyruvate + protein N-pros-phosphohistidine
-
-
-
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
ping-pong mechanism
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
bi-bi ping-pong mechanism
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phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
bi-bi ping-pong mechanism
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
in a second reaction step phosphate is transferred to the N-1 position of the imidazole ring of the histidine containing-protein (i.e. HPr), the phospho group of the intermediate phospho-enzyme I can also be transferred to pyruvate or 2-oxobutyrate
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
in a first reaction step phosphate is transferred to the N-3 position of the imidazole ring of histidine
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
overview on mechanism
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
enzyme I of the phosphotransferase system (cf. EC 2.7.1.69 protein-N-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
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37278-17-4
-
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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
alpha-ketobutyrate + phosphorylated histidine-containing protein
phosphoenolbutyrate + histidine-containing protein
-
-
-
-
?
beta-hydroxypyruvate + phosphorylated histidine-containing protein
? + histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
phosphoenolpyruvate + fructose
pyruvate + fructose 1-phosphate
-
no evidence for requirement of a phosphate carrier such as HPr (i.e. histidine-containing protein) for phosphorylation of fructose
-
?
phosphoenolpyruvate + fructose
pyruvate + fructose 1-phosphate
-
no evidence for requirement of a phosphate carrier such as HPr (i.e. histidine-containing protein) for phosphorylation of fructose
-
?
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
-
-
-
-
?
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 + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
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
-
in a first reaction step phosphate is transferred to the N-3 position of the imidazole ring of histidine
i.e. phospho-HPr
r
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
in a second reaction step phosphate is transferred to the N-1 position of the imidazole ring of the histidine containing-protein (i.e. HPr), the phospho group of the intermediate phospho-enzyme I can also be transferred to pyruvate or 2-oxobutyrate
-
-
r
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
r
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
-
-
-
-
?
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 + HPr
pyruvate + phospho-HPr
i.e. histidine-containing protein, phospho-HPr serves as a phosphoryl distributor to a number of different sugar-specific enzyme III/enzyme II complexes
i.e. phosphorylated histidine-containing protein
?
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
HPr, heat stable histidine containing protein, HPr(Ser-P) heat stable histidine containing protein phosphorylated at serine 46, HPr(His-P) heat stable histidine containing protein phosphorylated at histidine 15, HPr-P2 heat stable histidine containing protein doubly phosphorylated, HPr(S46D) heat stable histidine containing protein in which serine is replaced by asparate
-
-
?
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 + protein histidine
pyruvate + protein N-pros-phosphohistidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
HPr, heat stable histidine containing protein, HPr(Ser-P) heat stable histidine containing protein phosphorylated at serine 46, HPr(His-P) heat stable histidine containing protein phosphorylated at histidine 15, HPr-P2 heat stable histidine containing protein doubly phosphorylated, HPr(S46D) heat stable histidine containing protein in which serine is replaced by asparate
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
?
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
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
the enzyme belongs to the phosphoenolpyruvate:sugar phosphotransferase system, PTS, which is the major uptake system responsible for the transport of fructose, glucose, and sucrose in Corynebacterium glutamicum ATCC 13032, overview
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
the dimeric protein enzyme I is autophosphorylated on a histidine residue by PEP, followed by phosphoryl group transfer to the histidine phosphocarrier protein, HPr, overview
-
-
?
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
-
-
-
-
r
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
-
-
-
-
r
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
-
-
-
-
r
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
-
-
-
-
r
additional information
?
-
the enzyme can function as an adhesin, identification of host target molecules, overview
-
-
?
additional information
?
-
-
the enzyme can function as an adhesin, identification of host target molecules, overview
-
-
?
additional information
?
-
the bacterial phosphoenolpyruvate:sugar phosphotransferase system, PTS, consists of a cascade of several proteins involved in the uptake and phosphorylation of carbohydrates, and in signal transduction pathways, overview. The PTS involves a cascade of phosphoryl-transfer steps from phosphoenolpyruvate to sugar-specific enzyme II permeases via phosphointermediates of the general cytosolic non-sugar-specific phosphotransferase enzyme I and HPr
-
-
?
additional information
?
-
-
the bacterial phosphoenolpyruvate:sugar phosphotransferase system, PTS, consists of a cascade of several proteins involved in the uptake and phosphorylation of carbohydrates, and in signal transduction pathways, overview. The PTS involves a cascade of phosphoryl-transfer steps from phosphoenolpyruvate to sugar-specific enzyme II permeases via phosphointermediates of the general cytosolic non-sugar-specific phosphotransferase enzyme I and HPr
-
-
?
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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 + protein histidine
pyruvate + protein Npi-phospho-L-histidine
-
-
-
?
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
i.e. histidine-containing protein, phospho-HPr serves as a phosphoryl distributor to a number of different sugar-specific enzyme III/enzyme II complexes
i.e. phosphorylated histidine-containing protein
?
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
the enzyme belongs to the phosphoenolpyruvate:sugar phosphotransferase system, PTS, which is the major uptake system responsible for the transport of fructose, glucose, and sucrose in Corynebacterium glutamicum ATCC 13032, overview
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
the dimeric protein enzyme I is autophosphorylated on a histidine residue by PEP, followed by phosphoryl group transfer to the histidine phosphocarrier protein, HPr, overview
-
-
?
additional information
?
-
the enzyme can function as an adhesin, identification of host target molecules, overview
-
-
?
additional information
?
-
-
the enzyme can function as an adhesin, identification of host target molecules, overview
-
-
?
additional information
?
-
the bacterial phosphoenolpyruvate:sugar phosphotransferase system, PTS, consists of a cascade of several proteins involved in the uptake and phosphorylation of carbohydrates, and in signal transduction pathways, overview. The PTS involves a cascade of phosphoryl-transfer steps from phosphoenolpyruvate to sugar-specific enzyme II permeases via phosphointermediates of the general cytosolic non-sugar-specific phosphotransferase enzyme I and HPr
-
-
?
additional information
?
-
-
the bacterial phosphoenolpyruvate:sugar phosphotransferase system, PTS, consists of a cascade of several proteins involved in the uptake and phosphorylation of carbohydrates, and in signal transduction pathways, overview. The PTS involves a cascade of phosphoryl-transfer steps from phosphoenolpyruvate to sugar-specific enzyme II permeases via phosphointermediates of the general cytosolic non-sugar-specific phosphotransferase enzyme I and HPr
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
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
Mg2+
induces small conformational changes, large conformational changes with Mg2+ and phosphoenolpyruvate, swivelling mechanism, dimerization of the enzyme depends on its ligands
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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
-
-
HPr9-30 peptide
i.e. Ac-GWAEGLHARPASIFVRAATATG-CONH2, derived from HPrsc, spanning residues Gly-9 to Ala-30
-
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
DeoR-type transcriptional regulator SugR acts as a repressor for genes encoding the phosphoenolpyruvate:sugar phosphotransferase system, PTS, overview. Identification of the SugR binding motifs in ptsI by competitve EMSA studies, overview. The effectors fructose-1-phosphate, fructose-1,6-bisphosphate, and glucose-6-phosphate influence the binding activity of the SugR repressor
-
additional information
-
DeoR-type transcriptional regulator SugR acts as a repressor for genes encoding the phosphoenolpyruvate:sugar phosphotransferase system, PTS, overview. Identification of the SugR binding motifs in ptsI by competitve EMSA studies, overview. The effectors fructose-1-phosphate, fructose-1,6-bisphosphate, and glucose-6-phosphate influence the binding activity of the SugR repressor
-
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
-
additional information
enzyme PtsA binding peptides derived from its putative target molecules, i.e. AVVVNDANRTRK, ADDESPEMKPGX, TXQVSNHKNHTN, LDSIRIIVIRRI, ADGGVPV, and DQRPAXRRMYRA, inhibit pneumococcal adhesion in vitro to lung- and tracheal-derived cell lines. In addition, the tested peptides inhibit lung colonization after intranasal inoculation of mice with Streptococcus pneumoniae
-
additional information
-
enzyme PtsA binding peptides derived from its putative target molecules, i.e. AVVVNDANRTRK, ADDESPEMKPGX, TXQVSNHKNHTN, LDSIRIIVIRRI, ADGGVPV, and DQRPAXRRMYRA, inhibit pneumococcal adhesion in vitro to lung- and tracheal-derived cell lines. In addition, the tested peptides inhibit lung colonization after intranasal inoculation of mice with Streptococcus pneumoniae
-
additional information
design and development of specific drugs, which can be obtained from peptides or protein fragments able to interfere with the first reaction of the protein cascade: the phosphorylation of the HPr by the first enzyme, the so-called enzyme enzyme I, overview. Interaction and binding analysis by fluorescence and circular dichroism, thermodynamic parameters, detailed overview
-
additional information
-
design and development of specific drugs, which can be obtained from peptides or protein fragments able to interfere with the first reaction of the protein cascade: the phosphorylation of the HPr by the first enzyme, the so-called enzyme enzyme I, overview. Interaction and binding analysis by fluorescence and circular dichroism, thermodynamic parameters, detailed overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphoenolpyruvate
-
physiological concentrations of phosphoenolpyruvate and Mg2+ increase the amount of dimeric, active dephospho-enzyme I
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cholera
Plasma and Mucosal Immunoglobulin M, Immunoglobulin A, and Immunoglobulin G Responses to the Vibrio cholerae O1 Protein Immunome in Adults With Cholera in Bangladesh.
COVID-19
Renin-angiotensin system inhibitors and susceptibility to COVID-19 in patients with hypertension: a propensity score-matched cohort study in primary care.
Dental Caries
Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system.
Hyperglycemia
HEALTH-RELATED FUNCTIONALITY OF PHENOLIC-ENRICHED PEA SPROUTS IN RELATION TO DIABETES AND HYPERTENSION MANAGEMENT
Hypertension
HEALTH-RELATED FUNCTIONALITY OF PHENOLIC-ENRICHED PEA SPROUTS IN RELATION TO DIABETES AND HYPERTENSION MANAGEMENT
Hypertension
Renin-angiotensin system inhibitors and susceptibility to COVID-19 in patients with hypertension: a propensity score-matched cohort study in primary care.
Infections
A novel role for enzyme I of the Vibrio cholerae phosphoenolpyruvate phosphotransferase system in regulation of growth in a biofilm.
Infections
Effect of Bdellovibrio bacteriovorus infection on the phosphoenolpyruvate:sugar phosphotransferase system in Escherichia coli: evidence for activation of cytoplasmic proteolysis.
Metabolic Syndrome
Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields.
Neoplasms
Isozyme patterns of branched-chain amino acid transaminase in human tissues and tumors.
Ovarian Neoplasms
Association of angiotensin-converting enzyme I gene I/D polymorphism with endometrial but not with ovarian cancer.
Pneumonia
Streptococcus pneumoniae Cell-Wall-Localized Phosphoenolpyruvate Protein Phosphotransferase Can Function as an Adhesin: Identification of Its Host Target Molecules and Evaluation of Its Potential as a Vaccine.
Renal Insufficiency, Chronic
A pilot study on gene expression of endoplasmic reticulum unfolded protein response in chronic kidney disease.
Salmonella Infections
Understanding the multifaceted roles of the phosphoenolpyruvate: Phosphotransferase system in regulation of Salmonella virulence using a mutant defective in ptsI and crr expression.
Starvation
Characterization of eukaryotic-like kinase activity in Escherichia coli using the gene-protein database.
Whooping Cough
[Integration and intramolecular transposition of the TnBP3 Bordetella pertussis transposon in the Escherichia coli K-12 cells -- mutant for the phosphoenolpyruvate-dependent phosphotransferase system Hpr protein ]
Whooping Cough
[The influence of Bordetella pertussis bvgAS operon on formation and resolution of plasmid-chromosome cointegrates in Escherichia coli K12 mutants with damages in common components of the phosphoenolpyruvate:sugar phosphotransferase system]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of partial reactions
-
0.0054
histidine-containing protein
-
-
-
0.195 - 0.2
phosphoenolpyruvate
-
37°C, pH 7.2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
UniProt
brenda
-
641887, 642496, 642497, 642499, 642505, 642509, 642511, 642512, 642514, 642515, 642516, 642518, 642520, 642521, 642524, 642527, 642528, 642530, 661169, 663221, 663326
-
-
brenda
-
-
-
brenda
several strains, overview
UniProt
brenda
serotype 2 strain D39 and strain WU2, and the unencapsulated derivative of strain WU2, namely strain 3.8DW, and the unencapsulated derivative of strain D39, namely strain R6, gene ptsI
UniProt
brenda
immunologically distinct from Escherichia coli or other Streptococci
-
-
brenda
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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
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the phosphoenolpyruvate phosphotransferase system (PTS) is ubiquitous in eubacteria and absent from eukaryotes
malfunction
metabolism
physiological function
malfunction
-
a deletion mutant exhibits increased surface accumulation compared with wild type Vibrio cholerae
malfunction
-
deficiency of enzyme I, EI, of the phosphoenolpyruvate phosphotransferase system in bacterial mutants lead to severe growth defects
malfunction
-
enzyme-deficient mutants with diminished intracellular survival show down-regulation of the PhoPQ regulon and Salmonella pathogenicity island and flagella genes
malfunction
-
enzyme-deficient mutants with diminished intracellular survival show down-regulation of the PhoPQ regulon and Salmonella pathogenicity island and flagella genes
-
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
metabolism
-
enzyme expression enables cells to grow with maltose, GlcNAc, sucrose, and trehalose
metabolism
-
enzyme expression enables cells to grow with maltose, GlcNAc, sucrose, and trehalose
-
physiological function
-
phosphorylation of histidine protein and FPr protein by enzyme I represses Vibrio cholerae biofilm formation in minimal medium supplemented with glucose or pyruvate
physiological function
-
phosphotransferase system is required for intestinal colonization and inhibits biofilm formation
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
physiological function
recombinant PtsA and anti-rPtsA antiserum inhibit adhesion of Streptococcus pneumoniae to cultured human lung adenocarcinoma A549 cells, epitope screening, overview. Homologous sequences are found in human BMPER, multimerin1, protocadherin19, integrinbeta4, epsin1 and collagen type VIIalpha1 proteins, all of which can be found in A549 cells except the latter. anti-rPtsA Antiserum reduces bacterial virulence in the intravenous inoculation mouse model. The surface-localized PtsA functions as an adhesin
physiological function
-
surface-localized enzyme functions as an adhesin for target host cells
physiological function
-
surface-localized enzyme functions as an adhesin for target host cells
-
physiological function
-
surface-localized enzyme functions as an adhesin for target host cells
-
Show AA Sequence and Transmembrane Helices (39100 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
130000 - 150000
-
gel filtration at room temperature
135000
38165
x * 38165, electrospray ionization mass spectrometry
44500
-
alpha2,beta,gamma, 2 * 44500 + 1 * 62000 + 1 * 64500, SDS-PAGE, N-terminal amino acid sequence
62000
-
alpha2,beta,gamma, 2 * 44500 + 1 * 62000 + 1 * 64500, SDS-PAGE, N-terminal amino acid sequence
64500
-
alpha2,beta,gamma, 2 * 44500 + 1 * 62000 + 1 * 64500, SDS-PAGE, N-terminal amino acid sequence
64600
70000
64600
-
2 * 64600, sedimentation equilibrium studies, monomer-dimer-tetramer association
64600
-
4 * 64600, sedimentation equilibrium studies, monomer-dimer-tetramer association
70000
-
monomer, gel filtration at 4-6°C
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
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
tetramer
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
?
x * 38165, electrospray ionization mass spectrometry
?
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
x * 38165, electrospray ionization mass spectrometry
-
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
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
-
2 * 64600, sedimentation equilibrium studies, monomer-dimer-tetramer association
dimer
-
2 * 57000-70000, gel filtration under denaturing conditions
dimer
-
2 * 57000-70000, sedimentation equilibrium centrifugation
dimer
-
2 * 57000-70000, gel filtration at 4-6°C
dimer
-
2 * 57000-70000, SDS-PAGE
dimer
dimerization is induced by phosphoenolpyruvate and Mg2+, dimer is the active form of enzyme
dimer
2 * 63165,sequence calculation, 2 * 70000-72000, recombinant untagged enzyme, SDS-PAGE, 2 * 62492-63932, recombinant untagged enzyme, mass spectrometry
tetramer
-
alpha2,beta,gamma, 2 * 44500 + 1 * 62000 + 1 * 64500, SDS-PAGE, N-terminal amino acid sequence
tetramer
-
4 * 64600, sedimentation equilibrium studies, monomer-dimer-tetramer association
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
phosphorylation of the N-terminal domain of enzyme I at His189 is catalyzed by the C-terminal domain of enzyme I
phosphoprotein
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
phosphorylation of the N-terminal domain of enzyme I at His189 is catalyzed by the C-terminal domain of enzyme I
-
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
phosphoprotein
the dimeric protein enzyme I is autophosphorylated on a histidine residue by PEP, followed by phosphoryl group transfer to the histidine phosphocarrier protein, HPr, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal domain of enzyme I in complex with phosphoenolpyruvate, sitting drop vapor diffusion method, using 0.1 M succinic acid (pH 7.0), and 15% PEG3350 at 20°C
structure of the phosphoenolpyruvate-binding enzyme I-domain PEP: sugar phosphotransferase system, sitting-drop, vapor-diffusion method
-
by vapour diffusion in hanging drops in presence of Mg2+, phosphoenolpyruvate and oxalate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C502A
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
active site mutant
-
H189A
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4
-
active site mutant
-
G356S
the mutant shows reduced dimerization affinity and lower autophosphorylation activity compared to the wild type enzyme
H189A
H189E
H186D
-
the phosphomimetic mutant of the N-terminal domain of enzyme I shows reduced thermal stability compared to the wild type enzyme
additional information
additional information
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, overview
additional information
-
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, overview
additional information
replacement of HPr and enzyme I 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 enzyme IIs of Escherichia coli, enhanced phosphorylation is achieved with Bacillus subtilis HPr mutants, overview
additional information
-
replacement of HPr and enzyme I 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 enzyme IIs of Escherichia coli, enhanced phosphorylation is achieved with Bacillus subtilis HPr mutants, overview
additional information
-
fusion protein of enzyme plus the remaining three subunits of glucose phosphotransferase system and Ala-Pro-rich linker sequences
additional information
-
overview on mutants
additional information
-
enzyme deletion mutant, alternative pathways
additional information
-
enzyme deletion mutants, virulence of
additional information
deletion mutant strains, e.g. strains LJ705 and SB2950, lacking enzyme I and HPr from the phosphoenolpyruvate:sugar phosphotransferase system produces the constitutive analogues enzyme I fructose and FPr, but does no grow in minimal medium supplemented with non-PTS sugars melibiose, glycerol, and maltose, in complete absence of Luria-Bertani broth, growth occurs after addition of AMP, metabolism and phenotypes, overview
additional information
-
deletion mutant strains, e.g. strains LJ705 and SB2950, lacking enzyme I and HPr from the phosphoenolpyruvate:sugar phosphotransferase system produces the constitutive analogues enzyme I fructose and FPr, but does no grow in minimal medium supplemented with non-PTS sugars melibiose, glycerol, and maltose, in complete absence of Luria-Bertani broth, growth occurs after addition of AMP, metabolism and phenotypes, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
tertiary structure remains intact, unfolding at lower and higher pH values
672645
additional information
-
effect of pH on hydrolysis of phospho-enzyme I complex
642504
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26 - 46
depends on the presence of effectors like phosphoenolpyruvate and Mg2+, thermal denaturation is reversible
47.5
-
stable up to, phosphoenolpyruvate stabilizes, Mg2+ destabilizes
additional information
additional information
-
thermodynamic properties
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile in purified state, sensitive to sulfhydryl reagents
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 0.05 M potassium phosphate buffer, pH 6.5, 0.2 mM dithioerythritol, 1 mM EDTA, several months
-
-18°C, 0.1 M potassium phosphate buffer, or 0.01 M Tris buffer, pH 6.5, 1 mM EDTA, 0.5 mM dithioerythritol, 5 mM MgCl2, 2-3 months stable
-
-20°C, 10 mM potassium phosphate buffer, pH 7.5, 0.1 M KCl, 20% glycerol, no significant loss of activity in several months
-
-20°C, 25 mM sodium phosphate buffer, pH 7.2, 1 mM NaN3, dithiothreitol, stable for months, but instable in Tris buffer
-
-20°C, phosphate buffer, pH 7.0, protein concentration 1 mg/ml, stable for at least 14 months
-
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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
Ni-resin column chromatography and gel G-200 Superdex filtration
Ni2+-NTA column chromatography and gel filtration
of the recombinant protein
Talon metal affinity resin column chromatography or Strep-Tactin resin column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli K-12 and Rosetta (DE3) cells
expression in Escherichia coli
gene ptsI encoding the enzyme, DNA and amino acid sequence determination and analysis, transcriptional organization and expression analysis, the genes encoding PTS components, namely ptsI, ptsH, and ptsF belong to the fructose-PTS gene cluster, whereas ptsG and ptsS are located in two separate regions. A gene coding for the DeoR-type transcriptional regulator sugR is involved in the transcriptional regulation of the fructose-PTS cluster genes of the C. glutamicum genome, overview. Organization of the intergenic region between the genes ptsI and cg2118 containing the binding motifs A and B
gene ptsI encoding the enzyme, DNA and amino acid sequence determination and analysis, transcriptional organization and expression analysis, the genes encoding PTS components, namely ptsI, ptsH, and ptsF belong to the fructose-PTS gene cluster, whereas ptsG and ptsS are located in two separate regions. A gene coding for the DeoR-type transcriptional regulator sugR is involved in the transcriptional regulation of the fructose-PTS cluster genes of the Corynebacterium glutamicum genome, overview. Organization of the intergenic region between the genes ptsI and cg2118 containing the binding motifs A and B
gene ptsI, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strain DH5alpha, recombinant expression in Escherichia coli strain BL21(DE3)pLysS
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
-
the N-terminal domain of enzyme I from Streptomyces coelicolor is expressed in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during growth on fructose the gene cluster HVO1495 to HVO1499, encoding homologs of the five bacterial phosphotransferase system components inclusive enzyme I is highly upregulated as a cotranscript
during growth on fructose the gene cluster HVO1495 to HVO1499, encoding homologs of the five bacterial phosphotransferase system components inclusive enzyme I is highly upregulated as a cotranscript
-
during growth on fructose the gene cluster HVO1495 to HVO1499, encoding homologs of the five bacterial phosphotransferase system components inclusive enzyme I is highly upregulated as a cotranscript
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
the enzyme is a target for antibacterial drugs. These drugs can be obtained from peptides or protein fragments able to interfere with the first reaction of the protein cascade: the phosphorylation of the HPr by the first enzyme, the so-called enzyme enzyme I, overview
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
medicine
-
virulence of enzyme deletion mutants
medicine
the enzyme can function as an adhesin, evaluation of its potential as a vaccine. Immunization with rPtsA protects mice against a sublethal intranasal and a lethal intravenous pneumococcal challenge. PtsA binding peptides derived from its putative target molecules can be considered for development of therapeutics, and rPtsA is a candidate for vaccine development
medicine
-
recombinant enzyme and anti-enzyme antiserum inhibit adhesion of Streptococcus pneumoniae to cultured human lung adenocarcinoma A-549 cells
medicine
-
recombinant enzyme and anti-enzyme antiserum inhibit adhesion of Streptococcus pneumoniae to cultured human lung adenocarcinoma A-549 cells
-
medicine
-
recombinant enzyme and anti-enzyme antiserum inhibit adhesion of Streptococcus pneumoniae to cultured human lung adenocarcinoma A-549 cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhu, 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 capricolum
Biochemistry
36
6947-6953
1997
Mycoplasma capricolum
brenda
Titgemeyer, F.; Walkenhorst, J.; Reizer, J.; Stuiver, M.H.; Cui, X.; Saier, M.H., Jr.
Identification and characterization of phosphoenolpyruvate:fructose phosphotransferase systems in three Streptomyces species
Microbiology
141
51-58
1995
Streptomyces coelicolor, Streptomyces griseofuscus, Streptomyces lividans
-
brenda
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
brenda
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
brenda
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
brenda
Kohlbrecher, D.; Eisermann, R.; Hengstenberg, W.
Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: molecular cloning and nucleotide sequence of the Staphylococcus carnosus ptsI gene and expression and complementation studies of the gene product
J. Bacteriol.
174
2208-2214
1992
Staphylococcus carnosus (P23533), Staphylococcus carnosus
brenda
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
brenda
Alpert, C.A.; Frank, R.; Stber, K.; Deutscher, J.; Hengstenberg, W.
Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis: purification and properties of the enzyme and characterization of its active center
Biochemistry
24
959-964
1985
Enterococcus faecalis
brenda
Vadeboncoeur, C.; Proulx, M.; Trahan, L.
Purification of proteins similar to HPr and enzyme I from the oral bacterium Streptococcus salivarius. Biochemical and immunochemical properties
Can. J. Microbiol.
29
1694-1705
1983
Streptococcus salivarius
brenda
Weigel, N.; Waygood, E.B.; Kukuruzinska, M.A.; Nakazawa, A.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of enzyme I from Salmonella typhimurium
J. Biol. Chem.
257
14461-14469
1982
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kukuruzinska, M.A.; Harrington, W.F.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Studies on the molecular weight and association of enzyme I
J. Biol. Chem.
257
14470-14476
1982
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Weigel, N.; Kukuruzinska, M.A.; Nakazawa, A.; Waygood, E.B.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Phosphoryl transfer reactions catalyzed by enzyme I of Salmonella typhimurium
J. Biol. Chem.
257
14477-14491
1982
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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
brenda
Brouwer, M.; Elferink, M.G.L.; Robillard, G.T.
Phosphoenolpyruvate-dependent fructose phosphotransferase system of Rhodopseudomonas sphaeroides: purification and physicochemical and immunochemical characterization of a membrane-associated enzyme I
Biochemistry
21
82-88
1982
Cereibacter sphaeroides
brenda
Durham, D.R.; Phibbs, P.V.
Fractionation and characterization of the phosphoenolpyruvate: fructose 1-phosphotransferase system from Pseudomonas aeruginosa
J. Bacteriol.
149
534-541
1982
Pseudomonas aeruginosa
brenda
Kukuruzinska, M.A.; Weigel, N.; Waygood, E.B.
Enzyme I from Salmonella typhimurium
Methods Enzymol.
90
431-436
1982
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
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
brenda
Saier, M.H.; Schmidt, M.R.; Lin, P.
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Kinetic characterization
J. Biol. Chem.
255
8579-8584
1980
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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
brenda
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
-
brenda
Jaffor Ullah, A.H.; Cirillo, V.P.
Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase system: purification and characterization of enzyme I
J. Bacteriol.
131
988-996
1977
Mycoplasma capricolum
brenda
Postma, P.W.; Roseman, S.
The bacterial phosphoenolpyruvate: sugar phosphotransferase system
Biochim. Biophys. Acta
457
213-257
1976
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Staphylococcus aureus
brenda
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
brenda
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
brenda
LiCalsi, C.; Crocenzi, T.S.; Freire, E.; Roseman, S.
Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium
J. Biol. Chem.
266
19519-19527
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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
brenda
Alice, A.F.; Perez-Martinez, G.; Sanchez-Rivas, C.
Phosphoenolpyruvate phosphotransferase system and N-acetylglucosamine metabolism in Bacillus sphaericus
Microbiology
149
1687-1698
2003
Lysinibacillus sphaericus
brenda
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
brenda
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
brenda
Ginsburg, A.; Peterkofsky, A.
Enzyme I: The gateway to the bacterial phosphoenolpyruvate:sugar phosphotransferase system
Arch. Biochem. Biophys.
397
273-278
2002
Mycoplasma capricolum
brenda
Chung, T.L.; Farh, L.; Chen, Y.L.; Shiuan, D.
Molecular cloning and characterization of a unique 60 kDa/72 kDa antigen gene encoding enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system (PTS) of Mycoplasma hyopneumoniae
J. Biochem.
128
261-269
2000
Mycoplasma hyopneumoniae
brenda
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
brenda
Huebner, G.; Koenig, S.; Koch, M.H.J.; Hengstenberg, W.
Influence of Phosphoenolpyruvate and Magnesium Ions on the Quaternary Structure of Enzyme I of the Phosphotransferase System from Gram-Positive Bacteria
Biochemistry
34
15700-15703
1995
Staphylococcus carnosus (P23533), Staphylococcus carnosus
brenda
Kok, M.; Bron, G.; Erni, B.; Mukhija, S.
Effect of enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) on virulence in a murine model
Microbiology
149
2645-2652
2003
Haemophilus influenzae, Salmonella enterica subsp. enterica serovar Typhimurium, Staphylococcus aureus (P51183), Staphylococcus aureus
brenda
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
brenda
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
brenda
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
brenda
Sutrina, S.L.; Alleyne, L.; Hoyte, K.; Blenman, M.
Effect of replacing the general energy-coupling proteins of the PEP:Sugar phosphotransferase system of Salmonella typhimurium with their fructose-inducible counterparts on utilization of the PTS sugar glucitol
Microbiology
148
3857-3864
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Cochu, A.; Vadeboncoeur, C.; Moineau, S.; Frenette, M.
Genetic and biochemical characterization of the phosphoenolpyruvate:glucose/mannose phosphotransferase system of Streptococcus thermophilus
Appl. Environ. Microbiol.
69
5423-5432
2003
Streptococcus thermophilus
brenda
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
brenda
Gonzalez, C.F.; Stonestrom, A.J.; Lorca, G.L.; Saier, M.H., Jr.
Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases
Biochemistry
44
598-608
2005
Treponema denticola
brenda
Oberholzer, A.E.; Bumann, M.; Schneider, P.; Bachler, C.; Siebold, C.; Baumann, U.; Erni, B.
Crystal structure of the phosphoenolpyruvate-binding enzyme I-domain from the Thermoanaerobacter tengcongensis PEP:sugar phosphotransferase system (PTS)
J. Mol. Biol.
346
521-532
2005
Caldanaerobacter subterraneus subsp. tengcongensis
brenda
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
brenda
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
brenda
Casabon, I.; Couture, M.; Vaillancourt, K.; Vadeboncoeur, C.
Synthesis of HPr(Ser-P)(His-P) by enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system of Streptococcus salivarius
Biochemistry
45
6692-6702
2006
Bacillus subtilis (P08838), Bacillus subtilis, Streptococcus salivarius (P30299), Streptococcus salivarius
brenda
Hurtado-Gomez, E.; Fernandez-Ballester, G.; Nothaft, H.; Gomez, J.; Titgemeyer, F.; Neira, J.L.
Biophysical characterization of the enzyme I of the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system
Biophys. J.
90
4592-4604
2006
Streptomyces coelicolor (Q9KZP1), Streptomyces coelicolor
brenda
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
brenda
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
brenda
Marquez, J.; Reinelt, S.; Koch, B.; Engelmann, R.; Hengstenberg, W.; Scheffzek, K.
Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system
J. Biol. Chem.
281
32508-32515
2006
Staphylococcus carnosus (P23533), Staphylococcus carnosus
brenda
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
brenda
Hurtado-Gomez, E.; Abian, O.; Munoz, F.J.; Hernaiz, M.J.; Velazquez-Campoy, A.; Neira, J.L.
Defining the epitope region of a peptide from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system able to bind to the enzyme I
Biophys. J.
95
1336-1348
2008
Streptomyces coelicolor (Q9KZP1), Streptomyces coelicolor
brenda
Gaigalat, L.; Schlueter, J.P.; Hartmann, M.; Mormann, S.; Tauch, A.; Puehler, A.; Kalinowski, J.
The DeoR-type transcriptional regulator SugR acts as a repressor for genes encoding the phosphoenolpyruvate:sugar phosphotransferase system (PTS) in Corynebacterium glutamicum
BMC Mol. Biol.
8
104
2007
Corynebacterium glutamicum (Q8NP83), Corynebacterium glutamicum
brenda
Sutrina, S.L.; Inniss, P.I.; Lazarus, L.; Inglis, L.; Maximilien, J.
Replacing the general energy-coupling proteins of the phosphoenolpyruvate:sugar phosphotransferase system of Salmonella typhimurium with fructose-inducible counterparts results in the inability to utilize nonphosphotransferase system sugars
Can. J. Microbiol.
53
586-598
2007
Salmonella enterica subsp. enterica serovar Typhimurium (P0A249), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Jiang, L.; Cai, J.; Wang, J.; Liang, S.; Xu, Z.; Yang, S.T.
Phosphoenolpyruvate-dependent phosphorylation of sucrose by Clostridium tyrobutyricum ZJU 8235: evidence for the phosphotransferase transport system
Biores. Technol.
101
304-309
2010
Clostridium tyrobutyricum, Clostridium tyrobutyricum ZJU 8235
brenda
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
brenda
Domenech, R.; Martinez-Gomez, A.; Aguado-Llera, D.; Martinez-Rodriguez, S.; Clemente-Jimenez, J.; Velazquez-Campoy, A.; Neira, J.
Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system
Arch. Biochem. Biophys.
526
44-53
2012
Streptomyces coelicolor
brenda
Navdaeva, V.; Zurbriggen, A.; Waltersperger, S.; Schneider, P.; Oberholzer, A.; Baehler, P.; Baechler, C.; Grieder, A.; Baumann, U.; Erni, B.
Phosphoenolpyruvate: sugar phosphotransferase system from the hyperthermophilic Thermoanaerobacter tengcongensis
Biochemistry
50
1184-1193
2011
Caldanaerobacter subterraneus subsp. tengcongensis (Q8R7R4), Caldanaerobacter subterraneus subsp. tengcongensis, Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 / JCM 11007 / NBRC 100824 / MB4 (Q8R7R4)
brenda
Domenech, R.; Martinez-Rodriguez, S.; Velazquez-Campoy, A.; Neira, J.L.
Peptides as inhibitors of the first phosphorylation step of the Streptomyces coelicolor phosphoenolpyruvate: sugar phosphotransferase system
Biochemistry
51
7393-7402
2012
Streptomyces coelicolor, Streptomyces coelicolor CECT 3243
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
Houot, L.; Chang, S.; Pickering, B.; Absalon, C.; Watnick, P.
The phosphoenolpyruvate phosphotransferase system regulates Vibrio cholerae biofilm formation through multiple independent pathways
J. Bacteriol.
192
3055-3067
2010
Vibrio cholerae serotype O1
brenda
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
brenda
Pickl, A.; Johnsen, U.; Schoenheit, P.
Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase
J. Bacteriol.
194
3088-3097
2012
Haloferax volcanii, Haloferax volcanii H26
brenda
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
brenda
Romero-Beviar, M.; Martinez-Rodriguez, S.; Prieto, J.; Goormaghtigh, E.; Ariz, U.; Martinez-Chantar, M. de la L.; Gomez, J.; Neira, J.L.
The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state
Protein Eng. Des. Sel.
23
729-742
2010
Streptomyces coelicolor (Q9KZP1), Streptomyces coelicolor, Streptomyces coelicolor M145 (Q9KZP1)
brenda
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
brenda
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
brenda
Mizrachi Nebenzahl, Y.; Blau, K.; Kushnir, T.; Shagan, M.; Portnoi, M.; Cohen, A.; Azriel, S.; Malka, I.; Adawi, A.; Kafka, D.; Dotan, S.; Guterman, G.; Troib, S.; Fishilevich, T.; Gershoni, J.M.; Braiman, A.; Mitchell, A.M.; Mitchell, T.J.; Porat, N.; Goliand, I.; Chalifa Caspi, V.; Swiatlo, E.; Tal, M.; Ellis, R.; Elia, N.; Dagan, R.
Streptococcus pneumoniae cell-wall-localized phosphoenolpyruvate protein phosphotransferase can function as an adhesin: identification of its host target molecules and evaluation of its potential as a vaccine
PLoS ONE
11
e0150320
2016
Streptococcus pneumoniae (A0A0H2ZMY1), Streptococcus pneumoniae
brenda
Lee, K.; Yun, Y.; Kim, I.; Suh, J.
Dimerization facilitates the conformational transitions for bacterial phosphotransferase enzyme I autophosphorylation in an allosteric manner
FEBS Open Bio
7
1208-1216
2017
Escherichia coli (P08839)
brenda
Morabbi Heravi, K.; Altenbuchner, J.
Cross talk among transporters of the phosphoenolpyruvate-dependent phosphotransferase system in Bacillus subtilis
J. Bacteriol.
200
e00213-18
2018
Bacillus subtilis, Bacillus subtilis KM0
brenda
Lim, S.; Seo, H.; Jeong, J.; Yoon, H.
Understanding the multifaceted roles of the phosphoenolpyruvate phosphotransferase system in regulation of Salmonella virulence using a mutant defective in ptsI and crr expression
Microbiol. Res.
223-225
63-71
2019
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium UK1
-
brenda
Mizrachi Nebenzahl, Y.; Blau, K.; Kushnir, T.; Shagan, M.; Portnoi, M.; Cohen, A.; Azriel, S.; Malka, I.; Adawi, A.; Kafka, D.; Dotan, S.; Guterman, G.; Troib, S.; Fishilevich, T.; Gershoni, J.M.; Braiman, A.; Mitchell, A.M.; Mitchell, T.J.; Porat, N.; Goliand, I.; Chalifa Caspi, V.; Swiatlo, E.; Tal,
Streptococcus pneumoniae cell-wall-localized phosphoenolpyruvate protein phosphotransferase can function as an adhesin identification of its host target molecules and evaluation of its potential as a vaccine
PLoS ONE
11
e0150320
2016
Streptococcus pneumoniae, Streptococcus pneumoniae TIGR 4, Streptococcus pneumoniae WU2
brenda
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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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Release 2023.1 (January 2023)
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