ISOPRENOID SYNTHESIS IN ESCHERICHIA-COLI - SEPARATION AND PARTIAL-PURIFICATION OF 4 ENZYMES INVOLVED IN THE SYNTHESIS
ISOPRENOID SYNTHESIS IN ESCHERICHIA-COLI - SEPARATION AND PARTIAL-PURIFICATION OF 4 ENZYMES INVOLVED IN THE SYNTHESIS
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DOI:
10.1093/oxfordjournals.jbchem.a135600
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发表时间:
1986-05-01
影响因子:
2.7
通讯作者:
KATSUKI, H
中科院分区:
文献类型:
--
作者:
FUJISAKI, S;NISHINO, T;KATSUKI, H
Isopentenyl pyrophosphate (IPP) isomerase, farnesyl pyrophosphate (FPP) synthetase, octaprenyl pyrophosphate (OPP) synthetase and undecaprenyl pyrophosphate (UPP) synthetase were partially purified from Escherichia coli by DEAE-Toyopearl chromatography. FPP synthetase catalyzed the condensation of IPP with dimethylallyl pyrophosphate (DPP) as well as with geranyl pyrophoshate (GPP) to yield FPP as final product. OPP synthetase and UPP synthetase catalyzed the condensation of IPP with FPP to yield OPP and cis,trans-polyprenyl pyrophosphates (the C45-, C50-, and C55-compound), respectively. Neither DPP nor GPP acted as a priming substrate for either enzyme. These four enzymes required Mg2+ or Mn2+ for their activities. UPP synthetase required also Triton X-100 for its activity. The addition of Triton X-100 enhanced OPP synthetase, but it did not affect IPP isomerase and FPP synthetase. It seems possible that the combination of the four enzymes ensures the in vivo synthesis of long-chain isoprenoids in E. coli.