PROPERTIES OF COBALT-SUBSTITUTED BOVINE SERUM AMINE OXIDASE

被引:33
作者
AGOSTINELLI, E
MORPURGO, L
WANG, CQ
GIARTOSIO, A
MONDOVI, B
机构
[1] UNIV ROMA LA SAPIENZA,DEPT BIOCHEM SCI A ROSSI FANELLI,I-00185 ROME,ITALY
[2] CNR,CTR MOLEC BIOL,ROME,ITALY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 222卷 / 03期
关键词
D O I
10.1111/j.1432-1033.1994.tb18918.x
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
Half-copper-depleted and fully copper-depleted amine oxidase from bovine serum were reconstituted with either copper or cobalt. All samples were studied by high-sensitivity scanning calorimetry, by enzyme activity analysis, and by reactivity with phenylhydrazine. The calorimetric profile of the protein was strongly modified by the removal of a single Cu ion approximately to the same extent as by complete copper removal, in agreement with the loss of over 80% enzymic activity. The thermograms of metal-reconstituted species showed a marked similarity with that of the native enzyme, irrespective of whether copper or cobalt was present. Reactivity with phenylhydrazine and enzymic activity measurements showed that in cobalt-substituted amine oxidase the organic cofactor was reactive and the enzyme was catalytically competent, although kinetically less efficient. These observations agree both with previous findings on the protein half-site reactivity and with previous suggestions for a copper conformational role in bovine serum amine oxidase, namely of maintaining a functional conformation at the active site.
引用
收藏
页码:727 / 732
页数:6
相关论文
共 28 条
  • [1] BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
  • [2] CLONING AND SEQUENCING OF THE PEROXISOMAL AMINE OXIDASE GENE FROM HANSENULA-POLYMORPHA
    BRUINENBERG, PG
    EVERS, M
    WATERHAM, HR
    KUIPERS, J
    ARNBERG, AC
    AB, G
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1989, 1008 (02) : 157 - 167
  • [3] Brumby PE, 1967, METHOD ENZYMOL, V10, P473
  • [4] HYDROXYL RADICAL PRODUCTION IN THE REACTIONS OF COPPER-CONTAINING AMINE OXIDASES WITH SUBSTRATES
    CASTELLANO, FN
    HE, ZW
    GREENAWAY, FT
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1157 (02) : 162 - 166
  • [5] DIPATTI MCB, 1990, J BIOL CHEM, V265, P21016
  • [6] A CU(I)-SEMIQUINONE STATE IN SUBSTRATE-REDUCED AMINE OXIDASES
    DOOLEY, DM
    MCGUIRL, MA
    BROWN, DE
    TUROWSKI, PN
    MCINTIRE, WS
    KNOWLES, PF
    [J]. NATURE, 1991, 349 (6306) : 262 - 264
  • [7] GIARTOSIO A, 1988, BIOCHEM BIOPH RES CO, V54, P66
  • [8] STRUCTURE-FUNCTION STUDIES OF SUBSTRATE OXIDATION BY BOVINE SERUM AMINE OXIDASE - RELATIONSHIP TO COFACTOR STRUCTURE AND MECHANISM
    HARTMANN, C
    KLINMAN, JP
    [J]. BIOCHEMISTRY, 1991, 30 (18) : 4605 - 4611
  • [9] A NEW REDOX COFACTOR IN EUKARYOTIC ENZYMES - 6-HYDROXYDOPA AT THE ACTIVE-SITE OF BOVINE SERUM AMINE OXIDASE
    JANES, SM
    MU, D
    WEMMER, D
    SMITH, AJ
    KAUR, S
    MALTBY, D
    BURLINGAME, AL
    KLINMAN, JP
    [J]. SCIENCE, 1990, 248 (4958) : 981 - 987
  • [10] IDENTIFICATION OF TOPAQUINONE AND ITS CONSENSUS SEQUENCE IN COPPER AMINE OXIDASES
    JANES, SM
    PALCIC, MM
    SCAMAN, CH
    SMITH, AJ
    BROWN, DE
    DOOLEY, DM
    MURE, M
    KLINMAN, JP
    [J]. BIOCHEMISTRY, 1992, 31 (48) : 12147 - 12154