Information on EC 2.7.1.63 - polyphosphate-glucose phosphotransferase

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The expected taxonomic range for this enzyme is: Actinomycetales

EC NUMBER
COMMENTARY
2.7.1.63
-
RECOMMENDED NAME
GeneOntology No.
polyphosphate-glucose phosphotransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
with long chain polyphosphates, the reaction proceeds by a processive type mechanism, with short polyphosphates the mechanism is nonprocessive
-
(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
-
(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
glucose and phospohate substrate binding site structures
-
(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
glucose and phospohate substrate binding site structures
-
-
(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
Glycolysis / Gluconeogenesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
polyphosphate:D-glucose 6-phosphotransferase
Requires a neutral salt, e.g. KCl, for maximum activity. Also acts on glucosamine.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
inorganic polyphosphate/ATP-glucomannokinase
-
-
inorganic polyphosphate/ATP-glucomannokinase
-
-
-
PGPTase
-
-
-
-
phosphotransferase, polyphosphate-glucose
-
-
-
-
poly P glucokinase
-
-
poly(P) glucokinase
-
-
-
-
poly(P)/ATP-glucomannokinase
-
-
-
-
poly(P)/ATP-glucomannokinase
-
-
poly(P)/ATP-glucomannokinase
-
-
-
PolyP-dependent glucokinase
Q6M4B1
-
PolyP-dependent glucokinase
Q6M4B1
-
-
polyP-GK
-
-
-
-
polyphosphate glucokinase
-
-
-
-
polyphosphate glucokinase
-
-
polyphosphate-D-(+)-glucose-6-phosphotransferase
-
-
-
-
polyphosphate-dependent glucokinase
Q6M4B1
-
polyphosphate-dependent glucokinase
Q6M4B1
-
-
polyphosphate-glucose 6-phosphotransferase
-
-
-
-
polyphosphate/ATP-glucomannokinase
-
-
-
-
inorganic polyphosphate:D-glucose 6-phosphotransferase
-
-
-
-
additional information
-
the enzyme belongs to the poly(P)-dependent kinase family
additional information
-
the enzyme belongs to the poly(P)-dependent kinase family
-
CAS REGISTRY NUMBER
COMMENTARY
9033-50-5
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
Q6M4B1
phylogenetic analysis
evolution
-
phylogenetic analysis
-
malfunction
Q6M4B1
a ppgK deletion mutant shows slowed growth in minimal medium with maltose as sole carbon source or under phosphate starvation. Moreover, in minimal medium containing 2 to 4% w/v glucose as carbon source, DELTAppgK grows to lower final biomass concentrations than the wild-type. Growth of a ppgK overexpressing strain is increased as compared to wild-type and empty vector control, respectively
malfunction
-
a ppgK deletion mutant shows slowed growth in minimal medium with maltose as sole carbon source or under phosphate starvation. Moreover, in minimal medium containing 2 to 4% w/v glucose as carbon source, DELTAppgK grows to lower final biomass concentrations than the wild-type. Growth of a ppgK overexpressing strain is increased as compared to wild-type and empty vector control, respectively
-
physiological function
Q6M4B1
presence of PPGK entails a growth advantage
physiological function
-
presence of PPGK entails a growth advantage
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(phosphate)120 + D-glucose
(phosphate)119 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)15 + D-glucose
(phosphate)14 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)20 + D-glucose
(phosphate)19 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)25 + D-glucose
(phosphate)24 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)4 + D-glucose
(phosphate)3 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)45 + D-glucose
(phosphate)44 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)5 + D-glucose
(phosphate)4 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)65 + D-glucose
(phosphate)64 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)75 + D-glucose
(phosphate)74 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
Q59568
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
ir
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
Mycobacterium sp., Mycobacterium jucho
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
Mycobacterium pellegrino
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
Nocardia minima
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
ir
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
tetrapolyphosphate appears to precede the formation of tripolyphosphate which accumulates as the ultimate product
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
no utilization of triphosphate or tetrapolyphosphate
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
polyphosphate is utilized nonprocessively with a preference for longer chains
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
the enzyme utilizes polyphosphate much more efficiently than it does ATP, with a turnover number/Kpolyphosphate to turnover number/KATP ratio of 2800
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
i.e. poly(P)n, no substrates are monophosphate, diphosphate or triphosphate
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
constitutive enzyme, enzyme is involved in metabolism of glucose
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
ir
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
ir
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-mannose
(phosphate)n-1 + D-mannose 6-phosphate
show the reaction diagram
-
slowly
-
-
?
(phosphate)n + D-mannose
(phosphate)n-1 + D-mannose 6-phosphate
show the reaction diagram
-
about 40% of the activity with glucose
-
-
?
(phosphate)n + D-mannose
(phosphate)n-1 + D-mannose 6-phosphate
show the reaction diagram
-
slowly
-
-
?
(phosphate)n + D-mannose
(phosphate)n-1 + D-mannose 6-phosphate
show the reaction diagram
-
about 40% of the activity with glucose
-
-
?
(phosphate)n + glucosamine
(phosphate)n-1 + D-glucosamine 6-phosphate
show the reaction diagram
-
rate similar to that of glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q59568
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Nocardia minima
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
no activity with ATP
-
-
-
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
the enzyme utilizes polyphosphate much more efficiently than it does ATP, with a turnover number/Kpolyphosphate to turnover number/KATP ratio of 2800
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
see also glucokinase, EC 2.7.1.2
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
no activity with ATP
-
-
-
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
about 30% of the activity with glucose
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
CTP + glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
CTP + glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
dATP + glucose
dADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
GTP + glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
GTP + glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
TTP + glucose
TDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
UTP + glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
UTP + glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
XTP + glucose
XDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
additional information
?
-
-
no activity with ATP
-
-
-
additional information
?
-
-
the enzyme also shows weak NAD kinase activity and fructokinase activity with polyphosphate or ATP
-
-
-
additional information
?
-
Q6M4B1
PolyP is highly preferred over ATP and other NTPs as substrate and with respect to the tested PolyPs differing in chain length. The protein is most active with PolyP75
-
-
-
additional information
?
-
-
no activity with ATP
-
-
-
additional information
?
-
-
the enzyme also shows weak NAD kinase activity and fructokinase activity with polyphosphate or ATP
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
Q6M4B1
-
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
constitutive enzyme, enzyme is involved in metabolism of glucose
-
-
?
(phosphate)n + D-glucose
(phosphate)n-1 + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation, about 30% as efficient as Mg2+
Co2+
-
divalent cations activate in the order of decreasing effectiveness: Mg2+, Mn2+, Co2+, Zn2+
Co2+
-
divalent cation required, 86% of the activity with Mg2+ for the polyphosphate-dependent activity and 30% of the activity with Mg2+ for ATP-dependent activity, 5 mM
Cu2+
-
divalent cation required, 11% of the activity with Mg2+ for the polyphosphate-dependent activity and no activation of ATP-dependent activity, 5 mM
Fe2+
-
divalent cation required, no activation of the polyphosphate-dependent activity and 15% of the activity with Mg2+ for ATP-dependent acticity, 5 mM
Mg2+
-
activation
Mg2+
-
activation; molar ratio poly(P)/Mg2+ above 0.5 inhibition below
Mg2+
-
requires 1-10 mM Mg2+
Mg2+
-
divalent cation required, maximal activition of polyphosphate-dependent glucokinase and ATP-dependent glucokinase activity, 5 mM
Mg2+
-
absolutely required as activator, best at 4 mM
Mn2+
-
activation, as effective as Mg2+
Mn2+
-
divalent cations activate in the order of decreasing effectiveness: Mg2+, Mn2+, Co2+, Zn2+
Mn2+
-
divalent cation required, 82% of the activity with Mg2+ for the polyphosphate-dependent activity and 88% of the activity with Mg2+ for ATP-dependent activity, 5 mM
Zn2+
-
activation, about 30% as efficient as Mg2+
Zn2+
-
divalent cations activate in the order of decreasing effectiveness: Mg2+, Mn2+, Co2+, Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
inhibits reaction with ATP
AMP
-
inhibits reaction with polyphosphate and glucose or ATP and glucose
ATP
-
at high concentrations competitive substrate inhibition with respect to glucose, ATP-dependent reaction
D-fructose 6-phosphate
-
inhibits reaction with polyphosphate and glucose or ATP and glucose
D-glucose
-
above 150 mM, substrate inhibition
D-glucose 6-phosphate
-
inhibits reaction with ATP
D-glucose 6-phosphate
-
inhibits reaction with polyphosphate and glucose
D-xylose
-
inhibits reaction with ATP
D-xylose
-
inhibits reaction with ATP; inhibits reaction with polyphosphate and glucose or ATP and glucose
NaCl
Nocardia minima
-
above 100 mM
Poly(P)
-
above 0.05 mM, substrate inhibition
Tetrapolyphosphate
-
inhibits reaction with ATP
tripolyphosphate
-
when present in excess together with Grahams salt at pH 7.2
Mg2+
-
molar ratio polyphosphate/Mg below 0.5, activation above, EDTA partially reverses
additional information
Q6M4B1
no effect by fructose 1,6-bisphosphate, xylose, cAMP, UDP glucose, and glucose 1,6-bisphosphate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
Q6M4B1
no effect by fructose 1,6-bisphosphate, xylose, cAMP, UDP glucose, and glucose 1,6-bisphosphate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
(phosphate)120
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.6
-
(phosphate)15
Q6M4B1
pH 7.0, temperature not specified in the publication
0.4
-
(phosphate)20
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.3
-
(phosphate)25
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.5
-
(phosphate)4
Q6M4B1
pH 7.0, temperature not specified in the publication
0.2
-
(phosphate)45
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.8
-
(phosphate)5
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.1
-
(phosphate)65
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.3
-
(phosphate)75
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.2
-
ATP
-
pH 7.0, 30C
6
-
ATP
Q6M4B1
pH 7.0, temperature not specified in the publication
3.9
-
CTP
Q6M4B1
pH 7.0, temperature not specified in the publication
0.06
-
D-glucose
-
pH 7.5, reaction with ATP
0.22
-
D-glucose
-
pH 8.6, reaction with ATP
0.28
-
D-glucose
-
pH 8.5, 37C
0.45
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 50C
0.48
-
D-glucose
-
pH 8.5, 30C, soluble enzyme
0.52
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 30C
0.6
-
D-glucose
-
pH 8.5, 30C, immobilized enzyme
0.77
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 30C
0.8
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 50C
0.85
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 9.0, 50C
0.94
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 9.0, 50C
0.5
-
glucose
-
pH 7.0, 30C
3.5
-
GTP
Q6M4B1
pH 7.0, temperature not specified in the publication
0.02
-
Hexametaphosphate
-
pH 7.0, 30C
0.8
-
ITP
Q6M4B1
pH 7.0, temperature not specified in the publication
0.15
-
Mannose
-
pH 7.0, 30C
0.175
-
Poly(P)
-
pH 8.5, 37C, in terms of acid-labile phosphate
0.033
-
poly(P10)
-
pH 7.5
-
0.082
-
poly(P10)
-
pH 8.5
-
0.037
-
poly(P138)
-
pH 7.5, 30C
-
0.0072
-
poly(P15)
-
pH 8.5, 30C, soluble enzyme
-
0.13
-
poly(P15)
-
pH 8.5, 30C, immobilized enzyme
-
0.025
-
poly(P209)
-
pH 7.5, 30C
-
3.8
-
poly(P30)
-
-
-
0.0012
-
poly(P31)
-
pH 7.5, 30C
-
0.0086
-
poly(P347)
-
pH 7.5, 30C
-
0.0046
-
poly(P35)
-
-
-
0.0088
-
poly(P35)
-
-
-
8e-05
-
poly(P400)
-
-
-
0.037
-
poly(P400)
-
-
-
0.0067
-
poly(P430)
-
pH 7.5, 30C
-
0.004
-
poly(P575)
-
pH 7.5, 30C
-
0.06
-
poly(P700)
-
-
-
0.002
-
poly(P724)
-
pH 7.5, 30C
-
0.013
-
poly(P75)
-
pH 7.5, 30C
-
0.012
-
poly(P8)
-
-
-
1.5
-
UTP
Q6M4B1
pH 7.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.3
-
(phosphate)120
Q6M4B1
pH 7.0, temperature not specified in the publication
-
6
-
(phosphate)15
Q6M4B1
pH 7.0, temperature not specified in the publication
8.5
-
(phosphate)20
Q6M4B1
pH 7.0, temperature not specified in the publication
-
10
-
(phosphate)25
Q6M4B1
pH 7.0, temperature not specified in the publication
-
2.5
-
(phosphate)4
Q6M4B1
pH 7.0, temperature not specified in the publication
8.3
-
(phosphate)45
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.2
-
(phosphate)5
Q6M4B1
pH 7.0, temperature not specified in the publication
-
11.6
-
(phosphate)65
Q6M4B1
pH 7.0, temperature not specified in the publication
-
15.4
-
(phosphate)75
Q6M4B1
pH 7.0, temperature not specified in the publication
-
0.4
-
ATP
Q6M4B1
pH 7.0, temperature not specified in the publication
0.1
-
CTP
Q6M4B1
pH 7.0, temperature not specified in the publication
33.6
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 30C
39.7
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 50C
92.6
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 50C
96.9
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 30C
129
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 9.0, 50C
136
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 9.0, 50C
108
-
glucose
-
pH 7.5
116
-
glucose
-
pH 8.6
1.3
-
GTP
Q6M4B1
pH 7.0, temperature not specified in the publication
3.3
-
ITP
Q6M4B1
pH 7.0, temperature not specified in the publication
270
-
poly(P30)
-
-
-
196
-
poly(P35)
-
-
-
163
-
poly(P400)
-
-
-
183
-
poly(P700)
-
-
-
87
-
poly(P8)
-
-
-
0.3
-
UTP
Q6M4B1
pH 7.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
113
-
(phosphate)120
Q6M4B1
pH 7.0, temperature not specified in the publication
0
10
-
(phosphate)15
Q6M4B1
pH 7.0, temperature not specified in the publication
283422
21.3
-
(phosphate)20
Q6M4B1
pH 7.0, temperature not specified in the publication
0
33.3
-
(phosphate)25
Q6M4B1
pH 7.0, temperature not specified in the publication
0
5
-
(phosphate)4
Q6M4B1
pH 7.0, temperature not specified in the publication
283423
41.5
-
(phosphate)45
Q6M4B1
pH 7.0, temperature not specified in the publication
0
0.3
-
(phosphate)5
Q6M4B1
pH 7.0, temperature not specified in the publication
0
116
-
(phosphate)65
Q6M4B1
pH 7.0, temperature not specified in the publication
0
51.3
-
(phosphate)75
Q6M4B1
pH 7.0, temperature not specified in the publication
0
0.07
-
ATP
Q6M4B1
pH 7.0, temperature not specified in the publication
22040
0.03
-
CTP
Q6M4B1
pH 7.0, temperature not specified in the publication
8829
64.4
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 30C
9202
88.5
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 30C
9202
116
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 50C
9202
126
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 50C
9202
145
-
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 9.0, 50C
9202
151
-
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 9.0, 50C
9202
0.4
-
GTP
Q6M4B1
pH 7.0, temperature not specified in the publication
11186
4.1
-
ITP
Q6M4B1
pH 7.0, temperature not specified in the publication
11874
0.2
-
UTP
Q6M4B1
pH 7.0, temperature not specified in the publication
17783
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11
-
ADP
Q6M4B1
pH 7.0, temperature not specified in the publication
15
-
AMP
Q6M4B1
pH 7.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
64.6
-
-
purified recombinant free cellulose-binding module fusion enzyme, pH 7.5, 50C
110
-
-
reaction with ATP and glucose
203
-
Q59568
polyphosphate-dependent activity
220
-
-
reaction with polyphosphate and glucose
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
8.3
-
broad plateau
7.5
-
-
polyphosphate- and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
11
-
activity range, profile, overview. 40% of maximal activity at pH 7.5, 50C, 31% at pH 9.0, 50C, recombinant enzyme fused with a family 3 cellulose-binding module
5.7
8.4
Q6M4B1
84% activity at pH 6.4 in 50 mM MES and 73% activity at pH 8.4 in 50 mM glycylglycine
6
8.4
-
very little activity below pH 6.0 and above pH 8.4
6
9.5
-
pH 6.0: about 25% of maximal activity, pH 9.5: about 35% of maximal activity, polyphosphate-dependent and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
polyphosphate-dependent and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
80
-
activity range, profile, overview. 40% of maximal activity at 50C, maximal activity at 55C, at pH 7.5, recombinant enzyme fused with a family 3 cellulose-binding module
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Q6M4B1
the enzyme is a component of PolyP containing granular (voluntin) in Corynebacterium glutamicum
-
Manually annotated by BRENDA team
additional information
-
the enzyme is a component of PolyP containing granular (voluntin) in Corynebacterium glutamicum
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Arthrobacter sp. (strain KM)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29000
-
-
SDS-PAGE
59000
-
Nocardia minima
-
gel filtration
64000
-
-
gel filtration
66000
-
-
gel filtration
67800
-
Q6M4B1
recombinant detagged enzyme, gel filtration
113000
-
-
sucrose density gradient centrifugation
275000
280000
-
non-denaturing PAGE, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 34000, SDS-PAGE
?
Q59568
x * 27400, calculation from nucleotide sequence; x * 33000, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE
-
homodimer
Q6M4B1
2 * 26700, about, sequence calculation
homodimer
-
2 * 26700, about, sequence calculation
-
additional information
-
structure modeling of the C-terminal and N-terminal domains, and large and small domains, respectively
additional information
Q6M4B1
PolyP supports the formation of homodimers, the active form of PPGK
additional information
-
structure modeling of the C-terminal and N-terminal domains, and large and small domains, respectively
-
additional information
-
PolyP supports the formation of homodimers, the active form of PPGK
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, cyrstallization drop on a silconized coverslip by mixing of 0.003 ml protein solution consisting of 10 mg/ml protein in 10 mM glucose, and 10 mM potassium phosphate, pH 7.0, with an equal volume of mother liquor composed of 2.0 M ammonium sulfate, 2% v/v PEG 400, and 0.1 M HEPES, pH 8.0, cyrstals are soaked in several heavy atom derivative solutions containing 1 mM of UO2Ac2, 10 mM AgNO3, 10 mM GdCl2, 1 mM HgCl2, 10 mM K2Pt(CN)4, 2 mM TmCl2, or 1 mM EuCl3 in 0.1 M Tris-HCl at different pH-values, dependent on the heavy atom salt, for 20-60 min at 20C, X-ray diffraction structure determiination and analysis at 3.0 A resolution, modeling
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
t1/2: 24 h at 3C or at 37C plus 0.3 M KCl
5
7
-
24 h stable at 3C
8.1
8.4
-
immobilized enzyme is stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
40
Q6M4B1
purified recombinant enzyme, 100% remaining activity after 1 h
37
-
-
24 h, pH 4-5: precipitation and 80% of activity retained, above pH 5.5: inactivation within 24 h, 0.3 M KCl stabilizes
40
-
-
5 min, 50% loss of activity
50
-
Q6M4B1
purified recombinant enzyme, 12% remaining activity after 1 h
60
-
Q6M4B1
purified recombinant enzyme, no remaining activity after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dialysed enzyme preparations are largely inactive, Mg2+ restores activity
-
dialysis against distilled water for 10 h leads to decreased activity
-
enzyme immobilized on corn stover is stable for one months at pH 8.5, 30C
-
KCl, 0.3 M, stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
frozen, partially purified preparation, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from Escherichia coli in several steps
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and His-tag cleavage with factor Xa
Q6M4B1
recombinant enzyme
Q59568
partial
Nocardia minima
-
not separable from ATP-glucokinase
-
not separable from ATP-glucokinase; partial
-
recombinant enzyme fused with a family 3 cellulose-binding module 3.2fold from Escherichia coli strain BL21(DE3) in a one-step purification and immobilization on regenerated amorphous cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene GMK, expression in Escherichia coli strain BL21(DE3)
-
gene cg2091 or ppgK, sequence comparisons and phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
Q6M4B1
expression in Escherichia coli
-
orf Tfu_1811 overexpressed as protein fused with a family 3 cellulose-binding module in Escherichia coli strain BL21 (DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
immobilization of the recombinant cellulose-binding module fusion enzyme, which shows about 7.7fold increased catalytic turnover compared to the free enzyme