ADP-specific glucokinase

ADPGK
Identifiers
Aliases	ADPGK, 2610017G09Rik, ADP-GK, ADP-specific glucokinase, ADP-dependent glucokinase, ADP dependent glucokinase
External IDs	OMIM: 611861; MGI: 1919391; GeneCards: ADPGK
Enzyme activity
Gene location (Human)
Chr.	Chromosome 15 (human)
End	72,785,846 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	59,231,335 bp
RNA expression pattern
	Top expressed in
	oocyte; ; monocyte; ; secondary oocyte; ; granulocyte; ; spleen; ; bone marrow cell; ; blood; ; upper lobe of left lung; ; appendix; ; body of pancreas;
	Top expressed in
	secondary oocyte; ; bone marrow; ; yolk sac; ; cumulus cell; ; somite; ; proximal tubule; ; lip; ; blood; ; spermatocyte; ; molar;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	phosphotransferase activity, alcohol group as acceptor; transferase activity; metal ion binding; kinase activity; ADP-specific glucokinase activity;
Cellular component	endoplasmic reticulum; membrane; extracellular region; endoplasmic reticulum membrane;
Biological process	glycolytic process; phosphorylation; glucose metabolic process; canonical glycolysis; carbohydrate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	83440
	72141
	ENSG00000159322
	ENSMUSG00000025236
	Q9BRR6
	Q8VDL4
NM_031284; NM_001365223; NM_001365224; NM_001365225; NM_001365226;
	NM_001365227; NM_001365228; NM_001365229
	NM_028121; NM_001359282
NP_112574; NP_001352152; NP_001352153; NP_001352154; NP_001352155;
	NP_001352156; NP_001352157; NP_001352158
	NP_082397; NP_001346211
	Wikidata
View/Edit Human	View/Edit Mouse

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PMC	articles
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NCBI	proteins

ADP-specific glucokinase
ADP-specific glucokinase
Identifiers
EC no.	2.7.1.147
CAS no.	173585-07-4
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

ADP-specific glucokinase (EC 2.7.1.147) also known as ADP-dependent glucokinase is an enzyme that catalyzes the chemical reaction

ADP +

2D representation of the chemical structure of Q23905964.

D-glucose

AMP +

2D representation of the chemical structure of Q36461529.

glucose 6-phosphate

The enzyme characterised from Pyrococcus furiosus converts D-glucose to its monophosphate, glucose 6-phosphate, by transferring a phosphate group from the cofactor, adenosine diphosphate (ADP), which is converted to adenosine monophosphate (AMP).^[5] A similar enzyme has also been found in Thermococcus kodakarensis, where it acts on glucosamine as well as glucose.^[6]

In humans, the ADP-dependent glucokinase is encoded by the ADPGK gene.^[7]

Structural studies

Examples of the ADP-dependent glucokinase structure solved by x-ray crystallography include the enzyme from mouse PDB accession code 5CCF and Archaea PDB: 1GC5.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000159322 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025236 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Kengen SW, Tuininga JE, de Bok FA, Stams AJ, de Vos WM (Dec 1995). "Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus". The Journal of Biological Chemistry. 270 (51): 30453–7. doi:10.1074/jbc.270.51.30453. PMID 8530474.
↑ Aslam, Mehwish; Takahashi, Naoya; Matsubara, Kohei; Imanaka, Tadayuki; Kanai, Tamotsu; Atomi, Haruyuki (2018). "Identification of the glucosamine kinase in the chitinolytic pathway of Thermococcus kodakarensis". Journal of Bioscience and Bioengineering. 125 (3): 320–326. doi:10.1016/j.jbiosc.2017.10.005. PMID 29146530.
↑ Ronimus RS, Morgan HW (Mar 2004). "Cloning and biochemical characterization of a novel mouse ADP-dependent glucokinase". Biochemical and Biophysical Research Communications. 315 (3): 652–8. Bibcode:2004BBRC..315..652R. doi:10.1016/j.bbrc.2004.01.103. PMID 14975750.

External links

Human ADPGK genome location and ADPGK gene details page in the UCSC Genome Browser.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000159322 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025236 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Kengen SW, Tuininga JE, de Bok FA, Stams AJ, de Vos WM (Dec 1995). "Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus". The Journal of Biological Chemistry. 270 (51): 30453–7. doi:10.1074/jbc.270.51.30453. PMID 8530474.

[6] Aslam, Mehwish; Takahashi, Naoya; Matsubara, Kohei; Imanaka, Tadayuki; Kanai, Tamotsu; Atomi, Haruyuki (2018). "Identification of the glucosamine kinase in the chitinolytic pathway of Thermococcus kodakarensis". Journal of Bioscience and Bioengineering. 125 (3): 320–326. doi:10.1016/j.jbiosc.2017.10.005. PMID 29146530.

[pmid14975750-7] Ronimus RS, Morgan HW (Mar 2004). "Cloning and biochemical characterization of a novel mouse ADP-dependent glucokinase". Biochemical and Biophysical Research Communications. 315 (3): 652–8. Bibcode:2004BBRC..315..652R. doi:10.1016/j.bbrc.2004.01.103. PMID 14975750.

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Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)