Information on EC 2.7.1.199 - protein-Npi-phosphohistidine-D-glucose phosphotransferase

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 enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.199
-
RECOMMENDED NAME
GeneOntology No.
protein-Npi-phosphohistidine-D-glucose phosphotransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[protein]-Npi-phospho-L-histidine + D-glucose[side 1] = [protein]-L-histidine + D-glucose 6-phosphate[side 2]
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Glycolysis / Gluconeogenesis
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-Npi-phospho-L-histidine:D-glucose Npi-phosphotransferase
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[protein]-Npi-phospho-L-histidine + 2',3'-epoxypropyl beta-D-glucopyranoside
?
show the reaction diagram
-
pseudosubstrate
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose[side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + chloroacetyl beta-D-glucopyranoside
?
show the reaction diagram
-
pseudosubstrate
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 6-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucoside[side 1]
[protein]-L-histidine + methyl alpha-D-glucose 6-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + methyl alpha-glucopyranoside
[protein]-L-histidine + methyl alpha-glucopyranoside 6-phosphate
show the reaction diagram
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + methyl alpha-glucoside[side 1]
[protein]-L-histidine + methyl alpha-glucoside 6-phosphate[side 2]
show the reaction diagram
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + methyl-alpha-D-glucopyranoside
?
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
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
show the reaction diagram
[protein]-Npi-phospho-L-histidine + methyl alpha-D-glucoside[side 1]
[protein]-L-histidine + methyl alpha-D-glucose 6-phosphate[side 2]
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Zn2+ does not affect the activity of the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',3'-epoxypropyl beta-D-glucopyranoside
-
-
-
2-deoxy-D-glucose
-
inhibitor of isoform EIICBAGlc1
2-Nitrophenyl beta-D-glucoside
-
inhibitor of isoform EIICBAGlc2
4-nitrophenyl alpha-D-glucoside
-
inhibitor of isoform EIICBAGlc2
beta-D-glucopyranosyl isothiocyanate
-
-
-
beta-D-glucopyranosyl phenyl isothiocyanate
-
-
-
chloroacetyl beta-D-glucopyranoside
-
-
-
isopropyl-beta-D-thiogalactopyranoside
-
inhibitory above 0.075 mM
methyl 6,7-anhydro-DL-glycero-alpha-D-gluco-heptopyranoside
-
-
-
methyl 6-deoxy-6-isothiocyanate-alpha-D-glucopyranoside
-
-
-
methyl alpha-D-glucopyranoside
-
-
methyl alpha-D-glucoside
-
inhibitor of isoform EIICBAGlc2
methyl alpha-D-mannopyranoside
-
-
methyl beta-D-glucoside
-
inhibitor of isoforms EIICBAGlc1 and EIICBAGlc2
Salicin
-
inhibitor of isoform EIICBAGlc2
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
2',3'-epoxypropyl beta-D-glucopyranoside
-
at pH 7.5 and 30C
-
0.2
2-deoxy-D-glucose[side 1]
-
at pH 7.5, temperature not specified in the publication
-
0.7
chloroacetyl beta-D-glucopyranoside
-
at pH 7.5 and 30C
-
0.01 - 0.06
D-glucose[side 1]
0.04
D-mannose[side 1]
-
at pH 7.5, temperature not specified in the publication
0.006
methyl alpha-glucoside[side 1]
-
at pH 7.5, temperature not specified in the publication
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0397
2-deoxy-D-glucose
-
solubilized isoform EIICBAGlc1, at pH 7.5 and 37C
0.0285
2-Nitrophenyl beta-D-glucoside
-
solubilized isoform EIICBAGlc2, at pH 7.5 and 37C
0.0321
4-nitrophenyl alpha-D-glucoside
-
solubilized isoform EIICBAGlc2, at pH 7.5 and 37C
0.0349
methyl alpha-D-glucoside
-
solubilized isoform EIICBAGlc2, at pH 7.5 and 37C
0.0094 - 0.0218
methyl beta-D-glucoside
0.0179
Salicin
-
solubilized isoform EIICBAGlc2, at pH 7.5 and 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
2',3'-epoxypropyl beta-D-glucopyranoside
Escherichia coli
-
at pH 7.5 and 30C
-
0.0024
beta-D-glucopyranosyl phenyl isothiocyanate
Escherichia coli
-
at pH 7.5 and 30C
-
0.0013
chloroacetyl beta-D-glucopyranoside
Escherichia coli
-
at pH 7.5 and 30C
-
0.00007
methyl 6,7-anhydro-DL-glycero-alpha-D-gluco-heptopyranoside
Escherichia coli
-
at pH 7.5 and 30C
-
0.0009
methyl 6-deoxy-6-isothiocyanate-alpha-D-glucopyranoside
Escherichia coli
-
at pH 7.5 and 30C
-
0.0008
methyl alpha-D-glucopyranoside
Escherichia coli
-
at pH 7.5 and 30C
0.0008
methyl alpha-D-mannopyranoside
Escherichia coli
-
at pH 7.5 and 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.125
-
solubilized isoform EIICBAGlc2 after 381fold purification, at pH 7.5 and 37C
6.019
-
solubilized isoform EIICBAGlc1 after 255fold purification, at pH 7.5 and 37C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9600
-
x * 9600, SDS-PAGE
50645
-
2 * 50645, calculated from amino acid sequence
71543
-
x * 71543, calculated from amino acid sequence
80000
-
x * 80000, SDS-PAGE
106000
-
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 50645, calculated from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydroxylapatite column chromatography and Sephadex G-50 gel filtration
-
Ni-NTA agarose column chromatography
-
Ni-NTA agarose column chromatography and Superose 12 gel filtration
-
Ni2+-NTA column chromatography and Fractogel EMD DMAE Ion-exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli 1100, SR1305, SR1308, and ZSC113 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli HB101 cells
-
expressed in Escherichia coli strain W3110 and ZSC112DELTAG
-
expressed in Escherichia coli ZSC113 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is repressed by the DeoR-type regulator SugR, RamB, and GlxR
expression of the major ptsG transcript is induced by repressed by the Mlc protein
-
in the absence of glucose, ptsG expression is repressed by the repressor Mlc, while in the presence of glucose Mlc is inactivated by binding to the dephosphorylated EIIBGlc domain of the EIICBGlc during glucose transport
-
phospho-ArcA represses ptsG P1 transcription by decreasing the cAMP receptor protein binding
-
protein YeeI is involved in the regulation of gene expression by inactivating repressor Ml. The enzyme synthesis is increased 6.2fold after addition of 0.2% (w/v) D-glucose
-
the enzyme expression is higher in D-glucose media than in glycerol. A mutation in the mlc gene greatly enhances enzyme expression in a glycerol-grown culture but has no effect on enzyme expression during growth on D-glucose
-
the presence of GlcT protein enables constitutive expression of the glcA gene
-
the transcriptional regulators GntR1 and GntR2 activate the enzyme expression
the umgC mutation (which allows a strain mutated in the mannose phosphotransferase system to grow on glucosamine) enhances enzyme mRNA levels
transcription of ptsG is regulated by the repressor Mlc
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C461D
-
the mutant shows only weak repression of beta-xylosidase synthesis compared to the wild type enzyme
H620D
-
the mutant shows only weak repression of beta-xylosidase synthesis compared to the wild type enzyme
T324I
-
the mutant shows only weak repression of beta-xylosidase synthesis compared to the wild type enzyme
C461D
-
the mutant shows only weak repression of beta-xylosidase synthesis compared to the wild type enzyme
-
H620D
-
the mutant shows only weak repression of beta-xylosidase synthesis compared to the wild type enzyme
-
T324I
-
the mutant shows only weak repression of beta-xylosidase synthesis compared to the wild type enzyme
-
C421S
-
inactive
F37Y
-
the mutant shows reduced activity with D-glucose and therefore increased activity towards D-ribose
G176D
-
the mutant shows reduced activity with D-glucose and therefore increased activity towards D-ribose
G281D
-
the mutant shows reduced activity with D-glucose and therefore increased activity towards D-ribose
I283T
-
the mutant shows reduced activity with D-glucose and therefore increased activity towards D-ribose
L289Q
-
the mutant shows reduced activity with D-glucose and therefore increased activity towards D-ribose