Literature DB >> 11092916

Cloning and functional expression in Escherichia coli of a cDNA encoding cardenolide 16'-O-glucohydrolase from Digitalis lanata Ehrh.

J J Framm1, A Peterson, C Thoeringer, A Pangert, E Hornung, I Feussner, M Luckner, P Lindemann.   

Abstract

A clone of cardenolide 16'-O-glucohydrolase cDNA (CGH I) was obtained from Digitalis lanata which encodes a protein of 642 amino acids (calculated molecular mass 73.2 kDa). The amino acid sequence derived from CGH I showed high homology to a widely distributed family of beta-glucohydrolases (glycosyl hydrolases family 1). The recombinant CGH I protein produced in Escherichia coli had CGH I activity. CGH I mRNA was detected in leaves, flowers, stems and fruits of D. lanata.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 11092916     DOI: 10.1093/pcp/pcd060

Source DB:  PubMed          Journal:  Plant Cell Physiol        ISSN: 0032-0781            Impact factor:   4.927


  2 in total

1.  Cloning of beta-primeverosidase from tea leaves, a key enzyme in tea aroma formation.

Authors:  Masaharu Mizutani; Hidemitsu Nakanishi; Jun-ichi Ema; Seung-Jin Ma; Etsuko Noguchi; Misa Inohara-Ochiai; Masako Fukuchi-Mizutani; Masahiro Nakao; Kanzo Sakata
Journal:  Plant Physiol       Date:  2002-12       Impact factor: 8.340

2.  Expression of recombinant Digitalis lanata EHRH. cardenolide 16'-O-glucohydrolase in Cucumis sativus L. hairy roots.

Authors:  He-Ping Shi; Peter Lindemann
Journal:  Plant Cell Rep       Date:  2006-06-15       Impact factor: 4.570

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.