%A CHEN Anhe, LI Jiana, CHAI Yourong, WANG Rui, LU Jun
%T Cloning and sequence analysis of a mutation-type
cinnamate 4-hydroxylase gene from L. var. DC.
%0 Journal Article
%D 2008
%J Front. Agric. China
%J Frontiers of Agriculture in China
%@ 1673-7334
%R 10.1007/s11703-008-0047-x
%P 456-462
%V 2
%N 4
%U {https://academic.hep.com.cn/fag/EN/10.1007/s11703-008-0047-x
%8 2008-12-05
%X A 2431-bp full-length cinnamate 4-hydroxylase gene, BoC4H, was cloned from Brassica oleracea L. var. acephala DC.. It contains 2 introns. Its mRNA is 1715 bp, encoding a deduced 481-amino-acid polypeptide with wide homologies to C4Hs from other plants. It possesses cytochrome P450 conserved domains and motifs such as the haem-iron binding motif, the E-R-R triad, the T-containing binding pocket motif and the hinge motif necessary for optimal orientation of the enzyme. It also has most of the canonical C4H/CYP73A5-featured substrate-recognition sites (SRSs) and active site residues. However, owing to a single-base deletion at C2242 and subsequent frame shift within the 3′ coding region as compared with C4H genes from Arabidopsis thaliana and other plants, BoC4H shows a 36-aa deletion/variation at its C-terminus and the SRS6 motif together with active site residues therein are absent. Thus BoC4H may be of no function or low activity. BoC4H is a membrane protein and is probably associated with the endoplasmic reticulum. Its secondary structure is dominated by alpha helices and random coils. The Swiss-Model could not predict its tertiary structure. B. oleracea contains a C4H gene family with at least 5 members.