Britsch L et al. 1993
- Authors:
Britsch L. Dedio J. Saedler H. Forkmann G.
- Title:
Molecular characterization of flavanone 3 beta-hydroxylases. Consensus
sequence, comparison with related enzymes and the role of conserved
histidine residues.
- Reference location:
European Journal of Biochemistry. 217(2):745-54, 1993 Oct 15.
- Abstract:
A heterologous cDNA probe from Petunia hybrida was used to isolate
flavanone-3 beta-hydroxylase-encoding cDNA clones from carnation (Dianthus
caryophyllus), china aster (Callistephus chinensis) and stock (Matthiola
incana). The deduced protein sequences together with the known sequences
of the enzyme from P. hybrida, barley (Hordeum vulgare) and snapdragon
(Antirrhinum majus) enabled the determination of a consensus sequence
which revealed an overall 84% similarity (53% identity) of flavanone 3
beta-hydroxylases from the different sources. Alignment with the sequences
of other known enzymes of the same class and to related non-heme iron-(II)
enzymes demonstrated the strict genetic conservation of 14 amino acids, in
particular, of three histidines and an aspartic acid. The conservation of
the histidine motifs provides strong support for the possible conservation
of structurally similar iron-binding sites in these enzymes. The putative
role of histidines as chelators of ferrous ions in the active site of
flavanone 3 beta-hydroxylases was corroborated by diethyl-pyrocarbonate
modification of the partially purified recombinant Petunia enzyme.
This page is part of the
Snapdragon Home Page.
The URL of the Snapdragon Home Page is
http://www.mpiz-koeln.mpg.de/snapdragon/snapdragon.html
If you have any comments, additions or corrections to this page of general
interest you are invited to use the
Snapdragon Guest Book.
For personal comments please write to the author(s) of this page or to
Kurt Stueber.
This page has last been modified on May 26, 1997.