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
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
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Biosynthesis of antibiotics
-
-
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
COMMENTARY
LITERATURE
inorganic polyphosphate:D-glucose 6-phosphotransferase
-
-
-
-
PGPTase
-
-
-
-
phosphotransferase, polyphosphate-glucose
-
-
-
-
poly(P) glucokinase
-
-
-
-
poly(P)/ATP-glucomannokinase
-
-
-
-
polyP-GK
-
-
-
-
polyphosphate glucokinase
-
-
-
-
polyphosphate-D-(+)-glucose-6-phosphotransferase
-
-
-
-
polyphosphate-glucose 6-phosphotransferase
-
-
-
-
polyphosphate/ATP-glucomannokinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9033-50-5
-
GENERAL INFORMATION
ORGANISM
UNIPROT
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
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
P9WIN1
-
-
-
?
(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
P9WIN1
-
-
-
?
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
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
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
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
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]
SUBSTRATE
ORGANISM
UNIPROT
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
-
0.0072
poly(P15)
-
pH 8.5, 30C, soluble enzyme
-
0.13
poly(P15)
-
pH 8.5, 30C, immobilized enzyme
-
3.8
poly(P30)
-
-
-
0.0086
poly(P347)
-
pH 7.5, 30C
-
0.0046
poly(P35)
-
-
-
0.0088
poly(P35)
-
-
-
0.00008
poly(P400)
-
-
-
0.037
poly(P400)
-
-
-
0.0067
poly(P430)
-
pH 7.5, 30C
-
0.06
poly(P700)
-
-
-
0.012
poly(P8)
-
-
-
1.5
UTP
Q6M4B1
pH 7.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
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
14721
21.3
(phosphate)20
Q6M4B1
pH 7.0, temperature not specified in the publication
12238
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
8814
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
42450
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
4
0.03
CTP
Q6M4B1
pH 7.0, temperature not specified in the publication
60
64.4
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 30C
35
88.5
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 30C
35
116
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 7.5, 50C
35
126
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 7.5, 50C
35
145
D-glucose
-
recombinant immobilized cellulose-binding module fusion enzyme, pH 9.0, 50C
35
151
D-glucose
-
recombinant free cellulose-binding module fusion enzyme, pH 9.0, 50C
35
0.4
GTP
Q6M4B1
pH 7.0, temperature not specified in the publication
37
4.1
ITP
Q6M4B1
pH 7.0, temperature not specified in the publication
229
0.2
UTP
Q6M4B1
pH 7.0, temperature not specified in the publication
65
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64.6
-
purified recombinant free cellulose-binding module fusion enzyme, pH 7.5, 50C
110
-
reaction with ATP and glucose
203
P9WIN1
polyphosphate-dependent activity
220
-
reaction with polyphosphate and glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 8.3
-
broad plateau
7.5
-
polyphosphate- and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity
pH RANGE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
polyphosphate-dependent and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
-
SDS-PAGE
673712
30000
-
about, gel filtration
641746
59000
Nocardia minima
-
gel filtration
641747
64000
-
gel filtration
641753
66000
-
gel filtration
641755
67800
Q6M4B1
recombinant detagged enzyme, gel filtration
721367
113000
-
sucrose density gradient centrifugation
641743
275000 - 280000
-
non-denaturing PAGE, gel filtration
641744
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 34000, SDS-PAGE
?
P9WIN1
x * 33000, SDS-PAGE, x * 27400, calculation from nucleotide sequence
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
-
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
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
t1/2: 24 h at 3C or at 37C plus 0.3 M KCl
641743
5 - 7
-
24 h stable at 3C
641743
8.1 - 8.4
-
immobilized enzyme is stable
641744
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
Q6M4B1
purified recombinant enzyme, 100% remaining activity after 1 h
721367
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
641743
40
-
5 min, 50% loss of activity
641754
50
Q6M4B1
purified recombinant enzyme, 12% remaining activity after 1 h
721367
60
Q6M4B1
purified recombinant enzyme, no remaining activity after 5 min
721367
GENERAL STABILITY
ORGANISM
UNIPROT
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
LITERATURE
frozen, partially purified preparation, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
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
P9WIN1
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
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
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