Catalytic properties of an expressed and purified higher plant type ζ-carotene desaturase from Capsicum annuum

被引：37
作者：
Breitenbach, J
Kuntz, M
Takaichi, S
Sandmann, G
机构：
[1] Univ Frankfurt, Inst Bot, Biosynth Grp, D-60054 Frankfurt, Germany
[2] Univ Grenoble 1, Grenoble, France
[3] CNRS, Grenoble, France
[4] Nippon Med Sch, Biol Lab, Kawasaki, Kanagawa, Japan
来源：
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1999年 / 265卷 / 01期
关键词：
Capsicum annuum; zeta-carotene desaturase; isomeric substrate; lycopene isomers; quinone cofactor;
D O I：
10.1046/j.1432-1327.1999.00746.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：
The zeta-carotene desaturase from Capsicum annuum (EC 1.14.99.-) was expressed in Escherichia coli, purified and characterized biochemically. The enzyme acts as a monomer with lipophilic quinones as cofactors. K-m values for the substrate zeta-carotene or the intermediate neurosporene in the two-step desaturation reaction ore almost identical. Product analysis showed that different lycopene isomers are formed, including substantial amounts of the all-trans form, together with 7,7',9,9'-tetracis prolycopene via the corresponding neurosporene isomers. The application of different geometric isomers as substrates revealed that the zeta-carotene desaturase has no preference for certain isomers and that the nature of the isomers formed during catalysis depends strictly on the isomeric composition of the substrate.
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页码：376 / 383
页数：8
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