ADP-specific glucokinase

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 ${\displaystyle \rightleftharpoons }$ AMP + D-glucose 6-phosphate

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
Search PMC articles PubMed articles NCBI proteins

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)[1] Band 15q24.1 Start 72,751,294 bp[1] End 72,785,846 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 B Start 59,198,841 bp[2] End 59,231,335 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 83440 72141 Ensembl ENSG00000159322 ENSMUSG00000025236 UniProt Q9BRR6 Q8VDL4 RefSeq (mRNA) NM_031284 NM_001365223 NM_001365224 NM_001365225 NM_001365226 NM_001365227 NM_001365228 NM_001365229 NM_028121 NM_001359282 RefSeq (protein) NP_112574 NP_001352152 NP_001352153 NP_001352154 NP_001352155 NP_001352156 NP_001352157 NP_001352158 NP_082397 NP_001346211 Location (UCSC) Chr 15: 72.75 – 72.79 Mb Chr 9: 59.2 – 59.23 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

1. GRCh38: Ensembl release 89: ENSG00000159322 – Ensembl, May 2017
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.
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.

External links

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

Further reading

• 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.