Sun, L. ; Ruppert, M. ; Sheludko, Y. ; Warzecha, Heribert ; Zhao, Y. ; Stöckigt, J. (2008)
Purification, cloning, functional expression and characterization of perakine reductase: the first example from the AKR enzyme family, extending the alkaloidal network of the plant Rauvolfia.
In: Plant molecular biology, 67 (5)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Perakine reductase (PR) catalyzes an NADPH-dependent step in a side-branch of the 10-step biosynthetic pathway of the alkaloid ajmaline. The enzyme was cloned by a "reverse-genetic" approach from cell suspension cultures of the plant Rauvolfia serpentina (Apocynaceae) and functionally expressed in Escherichia coli as the N-terminal His(6)-tagged protein. PR displays a broad substrate acceptance, converting 16 out of 28 tested compounds with reducible carbonyl function which belong to three substrate groups: benzaldehyde, cinnamic aldehyde derivatives and monoterpenoid indole alkaloids. The enzyme has an extraordinary selectivity in the group of alkaloids. Sequence alignments define PR as a new member of the aldo-keto reductase (AKR) super family, exhibiting the conserved catalytic tetrad Asp52, Tyr57, Lys84, His126. Site-directed mutagenesis of each of these functional residues to an alanine residue results in >97.8% loss of enzyme activity, in compounds of each substrate group. PR represents the first example of the large AKR-family which is involved in the biosynthesis of plant monoterpenoid indole alkaloids. In addition to a new esterase, PR significantly extends the Rauvolfia alkaloid network to the novel group of peraksine alkaloids.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2008 |
| Autor(en): | Sun, L. ; Ruppert, M. ; Sheludko, Y. ; Warzecha, Heribert ; Zhao, Y. ; Stöckigt, J. |
| Art des Eintrags: | Bibliographie |
| Titel: | Purification, cloning, functional expression and characterization of perakine reductase: the first example from the AKR enzyme family, extending the alkaloidal network of the plant Rauvolfia. |
| Sprache: | Englisch |
| Publikationsjahr: | 2008 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Plant molecular biology |
| Jahrgang/Volume einer Zeitschrift: | 67 |
| (Heft-)Nummer: | 5 |
| Kurzbeschreibung (Abstract): | Perakine reductase (PR) catalyzes an NADPH-dependent step in a side-branch of the 10-step biosynthetic pathway of the alkaloid ajmaline. The enzyme was cloned by a "reverse-genetic" approach from cell suspension cultures of the plant Rauvolfia serpentina (Apocynaceae) and functionally expressed in Escherichia coli as the N-terminal His(6)-tagged protein. PR displays a broad substrate acceptance, converting 16 out of 28 tested compounds with reducible carbonyl function which belong to three substrate groups: benzaldehyde, cinnamic aldehyde derivatives and monoterpenoid indole alkaloids. The enzyme has an extraordinary selectivity in the group of alkaloids. Sequence alignments define PR as a new member of the aldo-keto reductase (AKR) super family, exhibiting the conserved catalytic tetrad Asp52, Tyr57, Lys84, His126. Site-directed mutagenesis of each of these functional residues to an alanine residue results in >97.8% loss of enzyme activity, in compounds of each substrate group. PR represents the first example of the large AKR-family which is involved in the biosynthesis of plant monoterpenoid indole alkaloids. In addition to a new esterase, PR significantly extends the Rauvolfia alkaloid network to the novel group of peraksine alkaloids. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Plant Biotechnology and Metabolic Engineering ?? fb10_botanik ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 17 Mär 2011 10:56 |
| Letzte Änderung: | 05 Mär 2013 09:46 |
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