ADP-specific glucokinase

Protein-coding gene in the species Homo sapiens
ADP-specific glucokinase
Identifiers
EC no.2.7.1.147
CAS no.173585-07-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
ADPGK
Identifiers
AliasesADPGK, 2610017G09Rik, ADP-GK, ADP-specific glucokinase, ADP-dependent glucokinase, ADP dependent glucokinase
External IDsOMIM: 611861; MGI: 1919391; HomoloGene: 41739; GeneCards: ADPGK; OMA:ADPGK - orthologs
Gene location (Human)
Chromosome 15 (human)
Chr.Chromosome 15 (human)[1]
Chromosome 15 (human)
Genomic location for ADPGK
Genomic location for ADPGK
Band15q24.1Start72,751,294 bp[1]
End72,785,846 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for ADPGK
Genomic location for ADPGK
Band9|9 BStart59,198,841 bp[2]
End59,231,335 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 9: 59.2 – 59.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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

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.
  • v
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Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
2.7.11: protein-serine/threonine
  • see serine/threonine-specific protein kinases
2.7.12: protein-dual-specificity
  • see serine/threonine-specific protein kinases
2.7.13: protein-histidine
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