Format

Send to

Choose Destination
FEBS Lett. 2001 Jun 15;499(1-2):15-20.

A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis.

Author information

1
Greenovation Pflanzenbiotechnologie GmBH, Freiburg, Germany. mschledz@greenovation.com

Abstract

The deduced polypeptide sequence of open reading frame slr1736 reveals homology to chlorophyll synthase and 1,4-dihydroxy-2-naphthoic acid phytyltransferase in Synechocystis sp. strain PCC 6803. In tocopherol and plastoquinone biosynthesis, a condensation reaction mechanistically similar to that of these two enzymes is performed. To analyze the function of this novel prenyltransferase, a deletion mutant of slr1736 was generated by homologous recombination. The mutant showed a markedly decreased tocopherol content, while plastoquinone levels remained unchanged. Since the aromatic precursor homogentisic acid accumulated in the mutant, the function of the enzyme was proven to be a novel tocopherol phytyltransferase.

PMID:
11418103
DOI:
10.1016/s0014-5793(01)02508-x
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center