Isolation of a new dual-functional caffeine synthase gene encoding an enzyme for the conversion of 7-methylxanthine to caffeine from coffee (Coffea arabica L.)

被引:75
作者
Mizuno, K
Okuda, A
Kato, M
Yoneyama, N
Tanaka, H
Ashihara, H
Fujimura, T
机构
[1] Univ Tsukuba, Inst Agr & Forest Engn, Tsukuba, Ibaraki 3058572, Japan
[2] Ochanomizu Univ, Grad Sch Humanities & Sci, Bunkyo Ku, Tokyo 1128610, Japan
[3] Ochanomizu Univ, Dept Biol, Fac Sci, Bunkyo Ku, Tokyo 1128610, Japan
关键词
coffee; caffeine; N-methyltransferase; 7-methylxanthine; S-adenosyl-L-methionine; theobromine;
D O I
10.1016/S0014-5793(02)03781-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
In coffee and tea plants, caffeine is synthesized from xanthosine via a pathway that includes three methylation steps. We report the isolation of a bifunctional coffee caffeine synthase (CCS1) clone from coffee endosperm by reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE) technique using previously reported sequence information for theobromine synthases (CTSs). The predicted amino acid sequences of CCS1 are more than 80% identical to CTSs and are about 40% similar to those of tea caffeine synthase (TCS1). Interestingly, CCS1 has dual methylation activity like tea TCS1. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:75 / 81
页数:7
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