Information on EC 2.7.3.9 - phosphoenolpyruvate-protein phosphotransferase

Word Map on EC 2.7.3.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.3.9
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate-protein phosphotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + protein histidine = pyruvate + protein N-pros-phosphohistidine
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + protein histidine = pyruvate + protein Npi-phospho-L-histidine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 hide
37278-17-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
strain ATCC 13032, gene ptsI
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
enzyme is fructose-inducible
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the phosphoenolpyruvate phosphotransferase system (PTS) is ubiquitous in eubacteria and absent from eukaryotes
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-ketobutyrate + phosphorylated histidine-containing protein
phosphoenolbutyrate + histidine-containing protein
show the reaction diagram
-
-
-
-
?
beta-hydroxypyruvate + phosphorylated histidine-containing protein
? + histidine-containing protein
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + fructose
pyruvate + fructose 1-phosphate
show the reaction diagram
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
show the reaction diagram
phosphoenolpyruvate + HPr
pyruvate + phospho-HPr
show the reaction diagram
phosphoenolpyruvate + protein histidine
pyruvate + protein N-pros-phosphohistidine
show the reaction diagram
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
show the reaction diagram
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
show the reaction diagram
pyruvate + phosphorylated histidine-containing protein
phosphoenolpyruvate + histidine-containing protein
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + histidine-containing protein
pyruvate + phosphorylated histidine-containing protein
show the reaction diagram
-
the enzyme is essential for the catabolism of many sugars by bacterial cells
-
-
?
phosphoenolpyruvate + HPr
pyruvate + phospho-HPr
show the reaction diagram
phosphoenolpyruvate + protein histidine
pyruvate + protein Npi-phospho-L-histidine
show the reaction diagram
A0A0H2ZMY1
-
-
-
?
phosphoenolpyruvate + protein histidine
pyruvate + protein phospho-L-histidine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4,5,6-triacetyloxy-9-oxoxanthen-3-yl)acetate
-
-
-
1,3,5-trihydroxy-2,4-bis(3-methylbut-2-enyl)xanthen-9-one
-
-
-
1,3,6,7-tetrahydroxy-2,8-bis(3-methylbut-2-enyl)xanthen-9-one
-
-
-
1,3,6-trihydroxy-7-methoxy-2,8-bis(3-methylbut-2-enyl)xanthen-9-one
-
-
-
1,3-bis(2-oxopropoxy)-9H-xanthen-9-one
-
-
1,6-dihydroxy-3,7-dimethoxy-2,8-bis(3-methylbut-2-enyl)xanthen-9-one
-
-
-
2,7-bis(2-aminoethoxy)xanthen-9-one
-
-
-
2,8-dihydroxy-1,6-dimethoxyxanthen-9-one
-
-
2-Hydroxy-3-butenoic acid
-
inactivation
2-[3-(prop-2-enylamino)propoxy]xanthen-9-one
-
-
-
5,7-diacetyl-6-(5-carboxy-6,7-dihydroxy-4-oxochromen-3-yl)-2,3-dihydroxy-9-oxoxanthene-1-carboxylic acid
-
-
6-chloro-2-(methylaminomethyl)xanthen-9-one
-
-
-
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
-
-
-
methyl 4-([(1-hydroxy-9-oxo-9H-xanthen-3-yl)oxy]methyl)benzoate
-
-
N-ethylmaleimide
-
irreversible inactivation
oxalate
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphoenolpyruvate
pyruvate
-
2 mM stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0054 - 0.031
Histidine-containing protein
-
12 - 39
HPr
-
0.18 - 0.68
phosphoenolpyruvate
additional information
additional information
-
kinetics of partial reactions
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
oxalate
-
inhibits the phosphorylated enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
530
-
37C, pH 7.0
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
HPr(Ser-P) and HPr(S46D) as substrates
5.8 - 8.5
-
less than 50% of maximal activity above and below
5.9 - 7.5
HPr(Ser-P) as substrate
5.9 - 8.5
HPr as substrate
6.5 - 8.5
HPr as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
bound to cytoplasmic membrane
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Staphylococcus carnosus (strain TM300)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27900
-
1 * 27900, calculated from amino acid sequence
28200
-
1 * 28200, sedimentation velocity analysis
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
63369
-
2 * 63369, sequence of cDNA
63489
-
2 * 63489, sequence of cDNA
64500
-
alpha2,beta,gamma, 2 * 44500 + 1 * 62000 + 1 * 64500, SDS-PAGE, N-terminal amino acid sequence
64600
-
2 * 64600, sedimentation equilibrium studies, monomer-dimer-tetramer association; 4 * 64600, sedimentation equilibrium studies, monomer-dimer-tetramer association
65000
-
2 * 65000, SDS-PAGE, gel filtration at 4-6C
72000
-
x * 72000, deduced from DNA-sequence
120100
recombinant untagged enzyme, mass spectrometry
130000 - 150000
-
gel filtration at room temperature
130000
135000
140000
-
size exclusion chromatography
160000
-
gel filtration
220000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
additional information
-
dephosphorylation
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 20C
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
-
crystals of the full length enzyme by vapour diffusion
-
putative structural models of the N- and C-terminal domains
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
tertiary structure remains intact, unfolding at lower and higher pH values
672645
6.5 - 7.5
-
dimerization of the enzyme depends on pH
674582
7
-
loss of activity above
642500
additional information
-
effect of pH on hydrolysis of phospho-enzyme I complex
642504
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 35
-
dimerization of the enzyme depends on the temperature
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile in purified state, sensitive to sulfhydryl reagents
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 0.05 M potassium phosphate buffer, pH 6.5, 0.2 mM dithioerythritol, 1 mM EDTA, several months
-
-18C, 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
-
-20C, 10 mM potassium phosphate buffer, pH 7.5, 0.1 M KCl, 20% glycerol, no significant loss of activity in several months
-
-20C, 25 mM sodium phosphate buffer, pH 7.2, 1 mM NaN3, dithiothreitol, stable for months, but instable in Tris buffer
-
-20C, lyophilized, indefinitely stable
-
-20C, phosphate buffer, pH 7.0, protein concentration 1 mg/ml, stable for at least 14 months
-
4C, lyophilized, or acidic solution, several months stable
-
several months at -80C, up to 1 h at 37C
storage solution contains 5 mM MgCl2 and phosphoenolpyruvate
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography and Superdex 200 gel filtration
-
from overproducing transformants
-
from overproducing transformants, also the N and C terminal domain of the enzyme
-
Ni-resin column chromatography and gel G-200 Superdex filtration
-
Ni2+ resin column chromatography, and gel filtration
-
Ni2+-NTA column chromatography and gel filtration
of the recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41 cells
-
expressed in Escherichia coli K-12 and Rosetta (DE3) cells
expressed in 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
-
in overproducing transformants, also the N- and C- terminal domain of the enzyme were cloned and expressed separately
-
mutant enzyme H186D is expressed in Escherichia coli C41 cells
-
overexpression of His-tagged protein in Escherichia coli
-
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
-
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G338D
-
significant loss of activity, no phosphorylation
G338E
-
significant loss of activity, no phosphorylation
G338H
-
significant loss of activity, diminishes phosphorylation
G338N
-
significant loss of activity
G338R
-
significant loss of activity, diminishes phosphorylation
G338V
-
significant loss of activity,decrease in phosphorylation
H15D
-
10-fold increase of Km, 1000-fold decrease of Vmax
H189Q
-
site directed mutagenesis
H186D
-
the phosphomimetic mutant of the N-terminal domain of enzyme I shows reduced thermal stability compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
Show AA Sequence (9904 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.