THE STRUCTURE OF THE QUINOPROTEIN ALCOHOL-DEHYDROGENASE OF ACETOBACTER-ACETI MODELED ON THAT OF METHANOL DEHYDROGENASE FROM METHYLOBACTERIUM-EXTORQUENS

被引:32
|
作者
COZIER, GE [1 ]
LAN, IG [1 ]
ANTHONY, C [1 ]
机构
[1] UNIV SOUTHAMPTON, SERC, CTR MOLEC RECOGNIT, DEPT BIOCHEM, SOUTHAMPTON SO16 7PX, HANTS, ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1042/bj3080375
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The 1.94 Angstrom structure of methanol dehydrogenase has been used to provide a model structure for part of a membrane quinohaemoprotein alcohol dehydrogenase. The basic superbarrel structure and the active-site region are retained, indicating essentially similar mechanisms of action, but there are considerable differences in the external loops, particularly those involved in formation of the shallow funnel leading to the active site.
引用
收藏
页码:375 / 379
页数:5
相关论文
共 50 条
  • [1] POSSIBLE FUNCTIONAL DOMAINS IN A QUINOPROTEIN ALCOHOL-DEHYDROGENASE FROM ACETOBACTER-ACETI
    INOUE, T
    SUNAGAWA, M
    MORI, A
    IMAI, C
    FUKUDA, M
    TAKAGI, M
    YANO, K
    JOURNAL OF FERMENTATION AND BIOENGINEERING, 1990, 70 (01): : 58 - 60
  • [2] THE REFINED STRUCTURE OF THE QUINOPROTEIN METHANOL DEHYDROGENASE FROM METHYLOBACTERIUM-EXTORQUENS AT 1.94 ANGSTROM
    GHOSH, M
    ANTHONY, C
    HARLOS, K
    GOODWIN, MG
    BLAKE, C
    STRUCTURE, 1995, 3 (02) : 177 - 187
  • [3] PURIFICATION AND PROPERTIES OF PARTICULATE ALCOHOL-DEHYDROGENASE FROM ACETOBACTER-ACETI
    ADACHI, O
    MIYAGAWA, E
    SHINAGAWA, E
    MATSUSHITA, K
    AMEYAMA, M
    AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1978, 42 (12): : 2331 - 2340
  • [4] Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens
    Cozier, GE
    Anthony, C
    BIOCHEMICAL JOURNAL, 1995, 312 : 679 - 685
  • [5] METHANOL DEHYDROGENASE FROM METHYLOBACTERIUM-EXTORQUENS AM1
    DAY, DJ
    ANTHONY, C
    METHODS IN ENZYMOLOGY, 1990, 188 : 210 - 216
  • [6] THE ROLE OF THE NOVEL DISULFIDE RING IN THE ACTIVE-SITE OF THE QUINOPROTEIN METHANOL DEHYDROGENASE FROM METHYLOBACTERIUM-EXTORQUENS
    AVEZOUX, A
    GOODWIN, MG
    ANTHONY, C
    BIOCHEMICAL JOURNAL, 1995, 307 : 735 - 741
  • [7] CLONING AND SEQUENCING OF THE GENE ENCODING THE 72-KILODALTON DEHYDROGENASE SUBUNIT OF ALCOHOL-DEHYDROGENASE FROM ACETOBACTER-ACETI
    INOUE, T
    SUNAGAWA, M
    MORI, A
    IMAI, C
    FUKUDA, M
    TAKAGI, M
    YANO, K
    JOURNAL OF BACTERIOLOGY, 1989, 171 (06) : 3115 - 3122
  • [8] BIOELECTROCATALYSIS BY ALCOHOL-DEHYDROGENASE FROM ACETOBACTER-ACETI ADSORBED ON BARE AND CHEMICALLY-MODIFIED ELECTRODES
    YANAI, H
    MIKI, K
    IKEDA, T
    MATSUSHITA, K
    DENKI KAGAKU, 1994, 62 (12): : 1247 - 1248
  • [9] PURIFICATION AND PROPERTIES OF COENZYME-INDEPENDENT ALCOHOL-DEHYDROGENASE FROM THE MEMBRANE-FRACTION OF ACETOBACTER-ACETI
    MURAOKA, H
    WATABE, Y
    OGASAWARA, N
    TAKAHASHI, H
    JOURNAL OF FERMENTATION TECHNOLOGY, 1982, 60 (01): : 41 - 50
  • [10] The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens
    Williams, PA
    Coates, L
    Mohammed, F
    Gill, R
    Erskine, PT
    Coker, A
    Wood, SP
    Anthony, C
    Cooper, JB
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2005, 61 : 75 - 79