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Information on EC 2.7.1.63 - polyphosphate-glucose phosphotransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WIN1

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EC Tree
IUBMB Comments
Requires a neutral salt, e.g. KCl, for maximum activity. Also acts on glucosamine.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WIN1
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
polyphosphate glucokinase, all1371, poly(p)/atp-glucomannokinase, pp-glk, polyp-gk, sco5059, polyp-glk, polyphosphate-glucose phosphotransferase, poly(p) glucokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inorganic polyphosphate:D-glucose 6-phosphotransferase
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PGPTase
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phosphotransferase, polyphosphate-glucose
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poly(P) glucokinase
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poly(P)/ATP-glucomannokinase
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polyP-GK
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polyphosphate glucokinase
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polyphosphate-D-(+)-glucose-6-phosphotransferase
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polyphosphate-glucose 6-phosphotransferase
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polyphosphate/ATP-glucomannokinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
in the polyphosphate-dependent reaction the enzyme follows an ordered bi bi sequential mechanism with polyphosphate binding to the enzyme first and glucose 6-phosphate dissociating last. The ATP-dependent glucokinase reaction is consistent with an ordered bi bi sequential mechanism, with ATP binding to the enzyme first and glucose 6-phosphate leaving last
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
polyphosphate:D-glucose 6-phosphotransferase
Requires a neutral salt, e.g. KCl, for maximum activity. Also acts on glucosamine.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-50-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
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-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
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-
-
?
(phosphate)10 + D-glucose
(phosphate)9 + D-glucose 6-phosphate
show the reaction diagram
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-
-
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?
(phosphate)35 + D-glucose
(phosphate)34 + D-glucose 6-phosphate
show the reaction diagram
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-
-
-
?
(phosphate)400 + D-glucose
(phosphate)399 + D-glucose 6-phosphate
show the reaction diagram
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-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
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-
-
-
?
CTP + glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
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-
-
-
?
GTP + glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
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-
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?
TTP + glucose
TDP + D-glucose 6-phosphate
show the reaction diagram
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-
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?
UTP + glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
-
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?
XTP + glucose
XDP + D-glucose 6-phosphate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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inhibits reaction with ATP
AMP
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inhibits reaction with polyphosphate and glucose or ATP and glucose
ATP
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at high concentrations competitive substrate inhibition with respect to glucose, ATP-dependent reaction
D-fructose 6-phosphate
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inhibits reaction with polyphosphate and glucose or ATP and glucose
D-glucose 6-phosphate
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inhibits reaction with polyphosphate and glucose
D-xylose
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 0.082
(phosphate)10
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0.0046
(phosphate)35
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0.00008
(phosphate)400
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0.88 - 1.4
ATP
0.06 - 0.22
D-glucose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
196
(phosphate)35
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163
(phosphate)400
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108 - 116
ATP
108 - 116
glucose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.6 - 7.4
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
203
polyphosphate-dependent activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27400
x * 27400, calculation from nucleotide sequence
33000
x * 33000, SDS-PAGE
30000
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2 * 30000, about, SDS-PAGE
66000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 30000, about, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Szymona, M.; Widomski, J.
A kinetic study on inorganic polyphosphate glucokinase from Mycobacterium tuberculosis H37RA
Physiol. Chem. Phys.
6
393-404
1974
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Ra / ATCC 25177
Manually annotated by BRENDA team
Hsieh, P.C.; Kowalczyk, T.H.; Phillips, N.F.
Kinetic mechanisms of polyphosphate glucokinase from Mycobacterium tuberculosis
Biochemistry
35
9772-9781
1996
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Hsieh, P.C.; Shenoy, B.C.; Samols, D.; Phillips, N.F.
Cloning, expression, and characterization of polyphosphate glucokinase from Mycobacterium tuberculosis
J. Biol. Chem.
271
4909-4915
1996
Mycobacterium tuberculosis (P9WIN1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIN1)
Manually annotated by BRENDA team
Phillips, N.F.B.; Hsieh, P.C.; Kowalczyk, T.H.
Polyphosphate glucokinase
Prog. Mol. Subcell. Biol.
23
101-125
1999
Corynebacterium xerosis, Mycobacterium tuberculosis, Mycolicibacterium phlei, Nocardia minima, Acidipropionibacterium acidipropionici, Propionibacterium freudenreichii subsp. shermanii
Manually annotated by BRENDA team