Study of IspH, a Key Enzyme in the Methylerythritol Phosphate Pathway Using Fluoro-Substituted Substrate Analogues-Reference-Cited by-同舟云学术

Study of IspH, a Key Enzyme in the Methylerythritol Phosphate Pathway Using Fluoro-Substituted Substrate Analogues

Published:2011-10-07 Issue:21 Volume:13 Page:5912-5915
ISSN:1523-7060
Container-title:Organic Letters
language:en
Short-container-title:Org. Lett.

Author:

Xiao Youli¹,Chang Wei-chen¹,Liu Hung-wen¹,Liu Pinghua¹

Affiliation:

1. Department of Chemistry, Boston University, Boston, Massachusetts 02215, United States, and Division of Medicinal Chemistry, College of Pharmacy, and Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, Texas 78712, United States

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ol202559r

Reference20 articles.

1. The discovery of a mevalonate-independent pathway for isoprenoid biosynthesis in bacteria, algae and higher plants†

2. Biosynthesis of isoprenoids via the non-mevalonate pathway

3. Unraveling the Mechanisms of Isoprenoid Biosynthetic Enzymes: Mechanistic Studies of the Early Stage Enzymes

4. Targeting Isoprenoid Biosynthesis for Drug Discovery: Bench to Bedside

5. Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) fromEscherichia coliis a [4Fe-4S] protein

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