Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 58, Issue 20, Pages 10911-10917Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf1021384
Keywords
Phenylalanine ammonia-lyase (PAL); cinnamate 4-hydroxylase (C4H); phenylpropanoid biosynthesis; garlic (Allium sativum)
Funding
- RDA, Republic of Korea [20080401-034-060-009-03-00]
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The cDNAs encoding phenylalanine ammonia-lyase (PAL) and cinnamate 4-hydroxylase (C4H) were cloned from garlic (Allium sativum) using reverse transcription-polymerase chain reaction (RT-PCR) with degenerate primers and 5' and 3' rapid amplification of cDNA ends (RACE) PCR. Amino acid sequence alignments showed that AsPAL and AsC4H have more than 70% amino acid identity with their homologues in other plants. The expression of AsPAL and AsC4H transcripts was highest in the roots but surprisingly low in the bulbils, where phenylpropanoid compounds are most concentrated. These results suggest that some phenylpropanoids are synthesized in the roots and subsequently transported to the bulbils of A. sativum.
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