Metanol dehidrogenaza (citohrom c)

Metanol dehidrogenaza (citohrom c)
Identifikatori
EC broj1.1.2.7
CAS broj37205-43-9
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

Metanol dehidrogenaza (citohrom c) (EC 1.1.2.7, MDH) je enzim sa sistematskim imenom metanol:citohrom c oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

primarni alkohol + 2 fericitohrom cL aldehid + 2 ferocitohrom cL + 2 H+

Ovaj enzim je periplazmična hinoproteinska alkoholna dehidrogenaza koja se javlja samo kod metilotrofnih bakterija. On koristi specifični citohrom cL kao acceptor i deluje na širok opseg primarnih alkohola, uključujući etanol, duodekanol, hloroetanol, cinamil alkohol, a takođe i formaldehid. Njegovu aktivnost stimuliše amonijak i metilamin. On se obično testira sa fenazin metosulfatom. Kao sve druge dehigenaze hinoproteinskog alkohola on ima strukturu propelera sa osam lopatica, jon kalcijuma vezan za PQQ u aktivnom mestu i neobičnu strukturu disulfidnog prstena u blizini PQQ. On se razlikuje od EC 1.1.2.8, alkoholne dehidrogenaze (citohroma c), po tome što ima visok afinitet za metanol, i što ima jednu dodatnu esencijalnu malu podjednicu nepoznate funkcije.

Reference

  1. ^ Anthony, C. & Zatman, L.J. (1964). „The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27”. Biochem. J. 92: 614—621. PMID 4378696. 
  2. ^ Anthony, C. & Zatman, L.J. (1967). „The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group”. Biochem. J. 104: 960—969. PMID 6049934. 
  3. ^ Duine, J.A., Frank, J. and Verweil, P.E.J. (1980). „Structure and activity of the prosthetic group of methanol dehydrogenase”. Eur. J. Biochem. 108: 187—192. PMID 6250827. 
  4. ^ Salisbury, S.A., Forrest, H.S., Cruse, W.B.T. and Kennard, O. (1979). „A novel coenzyme from bacterial primary alcohol dehydrogenases”. Nature (Lond.). 280: 843—844. PMID 471057. 
  5. ^ Cox, J.M., Day, D.J. and Anthony, C. (1992). „The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria”. Biochim. Biophys. Acta. 1119: 97—106. PMID 1311606. 
  6. ^ Blake, C.C., Ghosh, M., Harlos, K., Avezoux, A. and Anthony, C. (1994). „The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues”. Nat. Struct. Biol. 1: 102—105. PMID 7656012. 
  7. ^ Xia, Z.X., He, Y.N., Dai, W.W., White, S.A., Boyd, G.D. and Mathews, F.S. (1999). „Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution”. Biochemistry. 38: 1214—1220. PMID 9930981. 
  8. ^ Afolabi, P.R., Mohammed, F., Amaratunga, K., Majekodunmi, O., Dales, S.L., Gill, R., Thompson, D., Cooper, J.B., Wood, S.P., Goodwin, P.M. and Anthony, C. (2001). „Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL”. Biochemistry. 40: 9799—9809. PMID 11502173. 
  9. ^ Anthony, C. & Williams, P. (2003). „The structure and mechanism of methanol dehydrogenase”. Biochim. Biophys. Acta. 1647: 18—23. PMID 12686102. 
  10. ^ Williams, P.A., Coates, L., Mohammed, F., Gill, R., Erskine, P.T., Coker, A., Wood, S.P., Anthony, C. and Cooper, J.B. (2005). „The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens”. Acta Crystallogr. D Biol. Crystallogr. 61: 75—79. PMID 15608378. 

Literatura

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