In view of an investigation of the molecular mechanism of anthocyanin biosynthesis from Loropetalum chinense var. rubrum, a bioinformatical analysis has been made of the two chalcone synthase genes LcCHSs cloned from Loropetalum L. chinense var. rubrum. By adopting RT-PCR method, LcCHS1 and LcCHS2 genes of Loropetalum chinense var. rubrum have been cloned, with 1 170 BP the open reading frame (ORF) of LcCHS1, encoding 389 amino acids, and with 1 182 BP the ORF of LcCHS2, encoding 393 amino acids. The amino acid sequences identity of twoLcCHSs are above 83% to other plant CHSs, such as Camellia sinensis, Vitis vinifera, Arabidopsis thaliana, Nicotiana tabacum. The catalytic triad (Cys164, His303 and Asn336) and two important sequences of CHS enzyme, “RLMMYQ QGCFAGGTVLR”and“GVLFGFGPGL”, are highly conserved, indicating a functional conservation of CHS during evolution. Tertiary structure prediction shows that both LcCHSs can form homodimers, with the spatial structures of the two LcCHSs proteins being very similar.