Hinoprotein glukoza dehidrogenaza

Hinoprotein glukoza dehidrogenaza
Identifikatori
EC broj 1.1.5.2
CAS broj 81669-60-5
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
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PMC articles
PubMed articles
NCBI Protein search

Hinoprotein glukoza dehidrogenaza (EC 1.1.5.2, membranska glukozna dehidrogenaza, mGDH, glukozna dehidrogenaza (PQQ-zavisna), glukozna dehidrogenaza (pirolohinolin-hinon), hinoproteinska D-glukozna dehidrogenaza) je enzim sa sistematskim imenom D-glukoza:ubihinon oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

D-glukoza + ubihinon ⇌ {\displaystyle \rightleftharpoons } D-glukono-1,5-lakton + ubihinol

Ovaj integralni membranski protein sadrži PQQ kao prostetičku grupu. On takođe sadrži vezan ubihinon i Mg2+ ili Ca2+. Elektronski akceptor je membranski ubihinon.

Reference

  1. ↑ Yamada, M., Sumi, K., Matsushita, K., Adachi, O. and Yamada, Y. (1993). „Topological analysis of quinoprotein glucose-dehydrogenase in Escherichia coli and its ubiquinone-binding site”. J. Biol. Chem. 268: 12812-12817. PMID 8509415. 
  2. ↑ Dewanti, A.R. and Duine, J.A. (1998). „Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action”. Biochemistry 37: 6810-6818. PMID 9578566. 
  3. ↑ Duine, J.A., Frank, J. and Van Zeeland, J.K. (1979). „Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'”. FEBS Lett. 108: 443-446. PMID 520586. 
  4. ↑ Ameyama, M., Matsushita, K., Ohno, Y., Shinagawa, E. and Adachi, O. (1981). „Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria”. FEBS Lett. 130: 179-183. PMID 6793395. 
  5. ↑ Cozier, G.E. and Anthony, C. (1995). „Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens”. Biochem. J. 312: 679-685. PMID 8554505. 
  6. ↑ Cozier, G.E., Salleh, R.A. and Anthony, C. (1999). „Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine”. Biochem. J. 340: 639-647. PMID 10359647. 
  7. ↑ Elias, M.D., Tanaka, M., Sakai, M., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. (2001). „C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone”. J. Biol. Chem. 276: 48356-48361. PMID 11604400. 
  8. ↑ James, P.L. and Anthony, C. (2003). „The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli”. Biochim. Biophys. Acta 1647: 200-205. PMID 12686133. 
  9. ↑ Elias, M.D., Nakamura, S., Migita, C.T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. (2004). „Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase”. J. Biol. Chem. 279: 3078-3083. PMID 14612441. 
  10. ↑ Mustafa, G., Ishikawa, Y., Kobayashi, K., Migita, C.T., Elias, M.D., Nakamura, S., Tagawa, S. and Yamada, M. (2008). „Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase”. J. Biol. Chem. 283: 22215-22221. PMID 18550551. 

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

  • MeSH Quinoprotein+glucose+dehydrogenase
  • p
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TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6