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In this study, the full cDNA sequences of HcADH2 and HcADH3 were cloned from  Hedychium coronarium . The amino acid sequences encoded by them contained three most conserved motifs of short-chain alcohol dehydrogenase (ADH), namely NAD +  binding domain, TGxxx[AG]xG and active site YxxxK. The highest similarity between two genes and ADH from other plants was 70%. Phylogenetic analysis showed that they belonged to a member of the short-chain dehydrogenases/reductases 110C subfamily, but they were distinctly clustered in different clades. Real-time polymerase chain reaction analyses showed that  HcADH2  was specifically expressed in bract, and it was expressed higher in no-scented  Hedychium forrestii  than other  Hedychium  species, but was undetectable in  Hedychium coccineum .  HcADH3  was expressed higher in the lateral petal of the flower than in other vegetative organs, and it was expressed the most in  H. coronarium  that is the most scented among  Hedychium  species, and its expression levels peaked at the half opening stage.  HcADH2  and  HcADH3  had almost no significant expression in leaves, but  HcADH2  was expressed in response to external stimuli. The mechanical injury and methyl jasmonate (MeJA) treatment could induce expression of  HcADH2  in leaves, whereas  HcADH3  could have an induced expression only by MeJA. The recombinant HcADH3 protein, but not HcADH2, expressed in  Escherichia coli -catalysed conversion of geraniol into citral. It was speculated that HcADH3 had an induced expression in vegetative organ of  H. coronarium  and took part in monoterpenoid biosynthesis in  H. coronarium  flowers, but the role of HcADH2 is relevant only for defensive reactions.

Differential expression and functional analysis of two short-chain alcohol dehydrogenases/reductases in Hedychium coronarium