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; HomoloGene: 41739; GeneCards: ADPGK; OMA:ADPGK - orthologs
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 cells; ; 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
	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
PubMed	articles
NCBI	proteins

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

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

ADP + D-glucose

\rightleftharpoons

AMP + D-glucose 6-phosphate

Thus, the two substrates of this enzyme are ADP and D-glucose, whereas its two products are AMP and D-glucose 6-phosphate.

This enzyme belongs to the family of transferases, to be specific those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.

In humans, the ADP-dependent glucokinase is encoded by the ADPGK gene.^[5]

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1GC5.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000159322 – Ensembl, May 2017
^ ^a ^b ^c 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.
^ 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. 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.

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.
Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T (2005). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Research. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
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. doi:10.1016/j.bbrc.2004.01.103. PMID 14975750.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.

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

[refGRCm38Ensembl-2] 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.

[pmid14975750-5] 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. doi:10.1016/j.bbrc.2004.01.103. PMID 14975750.

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v t e 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)

ADP-specific glucokinase

Structural studies

References

External links

Further reading