메뉴 건너뛰기




Volumn 3, Issue 5, 2001, Pages 757-774

Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; CYTOCHROME C; GLUCOSE DEHYDROGENASE; MEMBRANE PROTEIN; METHANOL; PROTEIN DERIVATIVE; PYRROLOQUINOLINEQUINONE;

EID: 0035212690     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/15230860152664966     Document Type: Review
Times cited : (116)

References (72)
  • 7
    • 0014127919 scopus 로고
    • The microbial oxidation of methanol: The prosthetic group of alcohol dehydrogenase of Pseudomonas sp. M27; a new oxidoreductase prosthetic group
    • (1967) Biochem J , vol.104 , pp. 960-969
    • Anthony, C.1    Zatman, L.J.2
  • 10
    • 0017808443 scopus 로고
    • The dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila: Comparison with dye-linked methanol dehydrogenase
    • (1978) Biochem J , vol.169 , pp. 677-686
    • Bamforth, C.W.1    Quayle, J.R.2
  • 14
    • 0029609904 scopus 로고
    • Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens
    • (1995) Biochem J , vol.312 , pp. 679-685
    • Cozier, G.E.1    Anthony, C.2
  • 15
    • 0029043812 scopus 로고
    • The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens
    • (1995) Biochem J , vol.307 , pp. 375-379
    • Cozier, G.E.1    Giles, I.G.2    Anthony, C.3
  • 16
    • 0033564725 scopus 로고    scopus 로고
    • 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
    • (1999) Biochem J , vol.340 , pp. 639-647
    • Cozier, G.E.1    Salleh, R.A.2    Anthony, C.3
  • 22
    • 0034622429 scopus 로고    scopus 로고
    • 2+-assisted, direct hydride transfer, and rate-determining tautomerization of C5-reduced PQQ to PQQH2, in the oxidation of β-D-glucose by soluble, quinoprotein glucose dehydrogenase
    • (2000) Biochemistry , vol.39 , pp. 9384-9392
    • Dewanti, A.R.1    Duine, J.A.2
  • 24
    • 0025830659 scopus 로고
    • Quinoproteins - Enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophyl quinone
    • (1991) Eur J Biochem , vol.200 , pp. 271-284
    • Duine, J.A.1
  • 33
    • 0344219434 scopus 로고
    • Mode of binding of pyrroloquinoline quinone to glucose dehydrogenase from Acinetobacter calcoaceticus
    • edited by Jongejan JA and Duine JA Dordrecht: Kluwer Academic Publishers
    • (1989) PQQ and Quinoproteins , pp. 100-102
    • Gorisch, H.1    Geiger, O.2    Adler, M.3
  • 36
    • 78651151958 scopus 로고
    • Glucose dehydrogenase of Bacterium anitratum: An enzyme with a novel prosthetic group
    • (1964) J Biol Chem , vol.239 , pp. 3630-3639
    • Hauge, J.G.1
  • 37
    • 0002068483 scopus 로고
    • Investigations on the active site of glucose dehydrogenase from Pseudomonas fluorescens
    • edited by Jongejan JA and Duine JA. Dordrecht: Kluwer Academic Publishers
    • (1989) PQQ and Quinoproteins , pp. 87-96
    • Imanaga, Y.1
  • 43
    • 0031018070 scopus 로고    scopus 로고
    • Characterization of the genes encoding the three-component membranebound alcohol dehydrogeanse from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus
    • (1997) Appl Environ Microbiol , vol.63 , pp. 1131-1138
    • Kondo, K.1    Horinouchi, S.2
  • 44
    • 0029148093 scopus 로고
    • Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the three-component membrane-bound alcohol dehydrogenase from Acetobacter pasteurianus
    • (1995) J Bacteriol , vol.177 , pp. 5048-5055
    • Kondo, K.1    Beppu, T.2    Horinouchi, S.3
  • 53
    • 0030478428 scopus 로고    scopus 로고
    • Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus
    • (1996) Arch Biochem Biophys , vol.336 , pp. 42-48
    • Olsthoorn, A.J.1    Duine, J.A.2
  • 56
    • 0033522648 scopus 로고    scopus 로고
    • The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat
    • published erratum appears in J Mol Biol 292:191, 1999
    • (1999) J Mol Biol , vol.289 , pp. 319-333
    • Oubrie, A.1    Rozeboom, H.J.2    Kalk, K.H.3    Duine, J.A.4    Dijkstra, B.W.5
  • 59
    • 0041705251 scopus 로고    scopus 로고
    • Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: Cloning and sequencing of the genes encoding cytochrome c 550 and an adjacent acetaldehyde dehydrogenase
    • (1999) Microbiology , vol.145 , pp. 471-481
    • Schobert, M.1    Gorisch, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.