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Isopentenyl diphosphate isomerase deficiency in Synechocystis sp. strain PCC6803
Author(s) -
Ershov Yuri,
Gantt R.Raymond,
Cunningham Francis X.,
Gantt Elisabeth
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01516-7
Subject(s) - isomerase , synechocystis , plastid , cyanobacteria , biochemistry , terpenoid , strain (injury) , chemistry , enzyme , biology , stereochemistry , chloroplast , gene , bacteria , genetics , anatomy
Isopentenyl diphosphate isomerase (IPP isomerase) in many organisms and in plastids is central to isoprenoid synthesis and involves the conversion between IPP and dimethylallyl diphosphate (DMAPP). It is shown that Synechocystis PCC6803 is deficient in IPP isomerase activity, consistent with the absence in its genome of an obvious homologue for the enzyme. Incorporation of [1‐ 14 C]IPP in cell extracts, primarily into C 20 , occurs only upon priming with DMAPP in Synechocystis PCC6803 and in Synechococcus PCC7942. Isoprenoid synthesis in these cyanobacteria does not appear to involve interconversion of IPP and DMAPP, raising the possibility that they are not within the plastid evolutionary lineage.