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Information on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase and Organism(s) Mus musculus and UniProt Accession Q8VDL4

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EC Tree
IUBMB Comments
Requires Mg2+. The enzyme, characterized from a number of hyperthermophilic archaeal species, is highly specific for ADP. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.
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This record set is specific for:
Mus musculus
UNIPROT: Q8VDL4
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
adpgk, adp-dependent glucokinase, adp-pfk, adp-dependent kinase, tk1110, adp-gk, phpfk, adp-dependent hexokinase, adp-hk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-dependent glucokinase
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ADP-dependent glucokinase
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-
-
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ADP-specific glucokinase
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-
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ADP:D-glucose 6-phosphotransferase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ADP:D-glucose/D-glucosamine 6-phosphotransferase
Requires Mg2+. The enzyme, characterized from a number of hyperthermophilic archaeal species, is highly specific for ADP. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
173585-07-4
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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
ADP + D-fructose
AMP + D-fructose 6-phosphate
show the reaction diagram
10% of the activity with D-glucose
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-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
show the reaction diagram
ADP + D-mannose
AMP + D-mannose 6-phosphate
show the reaction diagram
20% of the activity with D-glucose
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-
?
CDP + D-glucose
CMP + D-glucose 6-phosphate
show the reaction diagram
12% of the activity with ADP
-
-
?
GDP + D-glucose
GMP + D-glucose 6-phosphate
show the reaction diagram
55% of the activity with ADP
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-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + D-glucose
AMP + D-glucose 6-phosphate
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
ADP-Mg2+ ratio of 1:1
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
required at 0.5 M for full enzyme activity
Mg2+
best at ADP-Mg2+ ratio of 1:1, excess Mg2+ is inhibitory
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg2+
excess Mg2+ is inhibitory, 55% inhibition at 55 mM, 41% at 15 mM, and 22% at 10 mM
NaCl
84% of maximal activity at 0.5 M, 48% of maximal activity at 1 M
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
ADP
at 0.8 mM and an ADP:Mg2+ ratio of 1:1, pH 7.0, 37°C
0.096
D-glucose
at below 0.35 mM, pH 7.0, 37°C
20
GDP
pH 7.0, 37°C
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.7
purified recombinant enzyme, pH 7.0, 37°C, substrate D-glucose
17
purified recombinant enzyme, pH 6.0, 37°C, substrate D-glucose
29.3
purified recombinant enzyme, pH 9.0, 37°C, substrate D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 6.5
bimodal optima at pH 5.8-6.5 and at 8.8-9.0
8.8 - 9
bimodal optima at pH 5.8-6.5 and at 8.8-9.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADPGK_MOUSE
496
0
53902
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51500
1 * 51500, recombinant enzyme, SDS-PAGE
60300
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 51500, recombinant enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain DH5alpha by nickel affinity and ion exchange chromatography, to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ronimus, R.S.; Morgan, H.W.
Cloning and biochemical characterization of a novel mouse ADP-dependent glucokinase
Biochem. Biophys. Res. Commun.
315
652-658
2004
Mus musculus (Q8VDL4), Mus musculus
Manually annotated by BRENDA team