Purification and characterization of pumpkin long-chain acyl-CoA oxidase

被引:5
作者
De Bellis, L
Giuntini, P
Hayashi, H
Hayashi, M
Nishimura, M
机构
[1] Univ Lecce, Dept Biol, I-73100 Lecce, Italy
[2] Dipartimento Biol Piante Agr, I-56124 Pisa, Italy
[3] Natl Inst Basic Biol, Dept Cell Biol, Okazaki, Aichi 4448585, Japan
关键词
D O I
10.1034/j.1399-3054.1999.106204.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Pumpkin (Cucurbita sp.) long-chain acyl-CoA oxidase (ACOX) (EC 1.3.3.6) was purified to homogeneity by hydrophobic interaction, hydroxyapatite, affinity, and anion exchange chromatographies. The purified isoenzyme is a dimeric protein, consisting of two apparently identical 72-kDa subunits. The protein is exclusively localized in glyoxysomes. The enzyme catalyzes selectively the oxidation of CoA esters of fatty acids with 12-18 C atoms and exhibits highest activity with C-14 fatty acids, but no activity with isobutyryl-CoA and isovaleryl-CoA (branched chain) or glutaryl-CoA (dicarboxylic). The enzyme is strongly inhibited by high concentrations of palmitoyl-CoA and weakly inhibited by high concentration of myristoyl-CoA. It is also inhibited by Triton X-100 at concentrations above 0.018% (w/v) the critical micellar concentration. The consequences of the substrate inhibition for the evaluation of long-chain ACOX activity in plant tissues are discussed.
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页码:170 / 176
页数:7
相关论文
共 22 条
[21]  
VANVELDHOVEN PP, 1992, J BIOL CHEM, V267, P20065
[22]   THE DUAL LOCATION OF BETA-OXIDATION ENZYMES IN GERMINATING PEA COTYLEDONS [J].
WOOD, C ;
BURGESS, N ;
THOMAS, DR .
PLANTA, 1986, 167 (01) :54-57