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Literature DB >> 23509611

Synthesis and evaluation of stable substrate analogs as potential modulators of cyclodiphosphate synthase IspF.

J Kipchirchir Bitok¹, Caren Freel Meyers.

Abstract

Stable IspF substrate analogs were synthesized. In the presence of substrate analogs, the E. coli IspF-MEP complex shows activities distinct from IspF, and bisphosphonates (BP) behave differently than their diphosphate (DP) counterparts. Bisphosphonate analogs activate and/or stabilize IspF, and only the closest structural substrate analog weakly inhibits the IspF-MEP complex.

Entities: Chemical Disease Gene Species

Year: 2013 PMID： 23509611 PMCID： PMC3597847 DOI： 10.1039/C2MD20175E

Source DB: PubMed Journal: Medchemcomm ISSN： 2040-2503 Impact factor: 3.597

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References

26 in total

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Synthesis and evaluation of stable substrate analogs as potential modulators of cyclodiphosphate synthase IspF.

1. Fluorescent inhibitors for IspF, an enzyme in the non-mevalonate pathway for isoprenoid biosynthesis and a potential target for antimalarial therapy.

2. The synthesis of oligoribonucleotides. II. Methoxymethylidene derivatives of ribonucleosides and 5'-ribonucleotides.

3. Creating isoprenoid diversity.

4. Structure of 2C-methyl-d-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids.

5. Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway.

6. Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate.

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