Ontology highlight
ABSTRACT:
SUBMITTER: Ghosh R
PROVIDER: S-EPMC3958759 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Ghosh Ritesh R Choi Bosung B Cho Byoung-Kwan BK Lim Hyoun-Sub HS Park Sang-Un SU Bae Hyeun-Jong HJ Natarajan Savithiry S Bae Hanhong H
TheScientificWorldJournal 20140226
Cinnamoyl-CoA reductase (CCR) is an important enzyme for lignin biosynthesis as it catalyzes the first specific committed step in monolignol biosynthesis. We have cloned a full length coding sequence of CCR from kenaf (Hibiscus cannabinus L.), which contains a 1,020-bp open reading frame (ORF), encoding 339 amino acids of 37.37 kDa, with an isoelectric point (pI) of 6.27 (JX524276, HcCCR2). BLAST result found that it has high homology with other plant CCR orthologs. Multiple alignment with other ...[more]