TY - JOUR
T1 - Cannabidiolic-acid synthase, the chemotype-determining enzyme in the fiber-type Cannabis sativa
AU - Taura, Futoshi
AU - Sirikantaramas, Supaart
AU - Shoyama, Yoshinari
AU - Yoshikai, Kazuyoshi
AU - Shoyama, Yukihiro
AU - Morimoto, Satoshi
N1 - Funding Information:
We thank Dr. Yuji Ito for determining amino acid sequences. This research was partially supported by Grants-in-Aid (Nos. 14771317 and 18780089 for F.T. and No. 10672108 for S.M.) from the Ministry of Education, Science, Sports, and Culture of Japan.
Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/6/26
Y1 - 2007/6/26
N2 - Cannabidiolic-acid (CBDA) synthase is the enzyme that catalyzes oxidative cyclization of cannabigerolic-acid into CBDA, the dominant cannabinoid constituent of the fiber-type Cannabis sativa. We cloned a novel cDNA encoding CBDA synthase by reverse transcription and polymerase chain reactions with degenerate and gene-specific primers. Biochemical characterization of the recombinant enzyme demonstrated that CBDA synthase is a covalently flavinylated oxidase. The structural and functional properties of CBDA synthase are quite similar to those of tetrahydrocannabinolic-acid (THCA) synthase, which is responsible for the biosynthesis of THCA, the major cannabinoid in drug-type Cannabis plants.
AB - Cannabidiolic-acid (CBDA) synthase is the enzyme that catalyzes oxidative cyclization of cannabigerolic-acid into CBDA, the dominant cannabinoid constituent of the fiber-type Cannabis sativa. We cloned a novel cDNA encoding CBDA synthase by reverse transcription and polymerase chain reactions with degenerate and gene-specific primers. Biochemical characterization of the recombinant enzyme demonstrated that CBDA synthase is a covalently flavinylated oxidase. The structural and functional properties of CBDA synthase are quite similar to those of tetrahydrocannabinolic-acid (THCA) synthase, which is responsible for the biosynthesis of THCA, the major cannabinoid in drug-type Cannabis plants.
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U2 - 10.1016/j.febslet.2007.05.043
DO - 10.1016/j.febslet.2007.05.043
M3 - Article
C2 - 17544411
AN - SCOPUS:34250179866
VL - 581
SP - 2929
EP - 2934
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 16
ER -