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Last update 08 May 2025

4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Last update 08 May 2025

Basic Info

Synonyms

ECK0030, HMBPP reductase, lytB

+ [1]

Introduction-

Drugs associated with 4-hydroxy-3-methylbut-2-enyl diphosphate reductase

IspH Inhibitors (Wistar Institute)

Target

4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Mechanism

4-hydroxy-3-methylbut-2-enyl diphosphate reductase inhibitors

Active Org.

The Wistar Institute

Originator Org.

The Wistar Institute

Active Indication

Bacterial Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with 4-hydroxy-3-methylbut-2-enyl diphosphate reductase

100 Translational Medicine associated with 4-hydroxy-3-methylbut-2-enyl diphosphate reductase

0 Patents (Medical) associated with 4-hydroxy-3-methylbut-2-enyl diphosphate reductase

139

Literatures (Medical) associated with 4-hydroxy-3-methylbut-2-enyl diphosphate reductase

31 Mar 2025·The FASEB Journal

Investigation of structural and dynamic properties of the Butyrophilin BTN3A1/BTN2A1 cytoplasmic complex by ¹⁹F solution NMR

Article

Author: Nguyen, Khiem ; Jin, Yiming ; Hsiao, Chia‐Hung Christine ; Wiemer, Andrew J. ; Vinogradova, Olga

AbstractButyrophilin 3A1 (BTN3A1) is an integral membrane protein capable of detecting phosphoantigens, like (E)‐4‐hydroxy‐3‐methyl‐but‐2‐enyl diphosphate (HMBPP), through its internal B30.2 domain. Detection of phosphoantigens leads to interactions with butyrophilin 2A1 and the subsequent activation of γδ‐T cells. Though crystallography and functional assays have been crucial for determining vital residues of the BTN3A1/HMBPP/BTN2A1 complex, the mechanism for signal transduction is still unclear. Here, we utilize 19F solution NMR to observe potential conformational and dynamic changes of specific residues upon complex formation. With point mutants of BTN3A1, we show that W421C, T449C, and T506C are residues that are influenced by HMBPP and BTN2A1 association, while T304C, G323C, C387, and C511 are not impacted. 19F labeling of W421C reduces the binding affinity of BTN2A1 toward BTN3A1/HMBPP, which indicates that W421 is located at the binding interface. T506 is located away from the phosphoantigen binding site, so its observable chemical shift perturbation suggests that there is a larger conformational change of the BTN3A1 B30.2 domain upon binding HMBPP and BTN2A1. The juxtamembrane residues, T304C, and G323C are not affected, showing that the changes are localized within the B30.2 domain of BTN3A1. Using BTN3A1 T449C, we were able to detect differential binding modes of synthetic HMBPP analogs, showing that it is possible to assess differences in protein conformations that are induced by binding of different ligands. Taken together, these findings illustrate the dynamic processes involved in phosphoantigen detection by the HMBPP receptor.

01 Jan 2025·The Plant Journal

Rapid and efficient in planta genome editing in sorghum using foxtail mosaic virus‐mediated sgRNA delivery

Article

Author: Cody, Jon P. ; Altpeter, Fredy ; Kausch, Albert P. ; Baysal, Can ; Voytas, Daniel F.

SUMMARYThe requirement of in vitro tissue culture for the delivery of gene editing reagents limits the application of gene editing to commercially relevant varieties of many crop species. To overcome this bottleneck, plant RNA viruses have been deployed as versatile tools for in planta delivery of recombinant RNA. Viral delivery of single‐guide RNAs (sgRNAs) to transgenic plants that stably express CRISPR‐associated (Cas) endonuclease has been successfully used for targeted mutagenesis in several dicotyledonous and few monocotyledonous plants. Progress with this approach in monocotyledonous plants is limited so far by the availability of effective viral vectors. We engineered a set of foxtail mosaic virus (FoMV) and barley stripe mosaic virus (BSMV) vectors to deliver the fluorescent protein AmCyan to track viral infection and movement in Sorghum bicolor. We further used these viruses to deliver and express sgRNAs to Cas9 and Green Fluorescent Protein (GFP) expressing transgenic sorghum lines, targeting Phytoene desaturase (PDS), Magnesium‐chelatase subunit I (MgCh), 4‐hydroxy‐3‐methylbut‐2‐enyl diphosphate reductase, orthologs of maize Lemon white1 (Lw1) or GFP. The recombinant BSMV did neither infect sorghum nor deliver or express AmCyan and sgRNAs. In contrast, the recombinant FoMV systemically spread throughout sorghum plants and induced somatic mutations with frequencies reaching up to 60%. This mutagenesis led to visible phenotypic changes, demonstrating the potential of FoMV for in planta gene editing and functional genomics studies in sorghum.

01 Dec 2024·Rice

YGL3 Encoding an IPP and DMAPP Synthase Interacts with OsPIL11 to Regulate Chloroplast Development in Rice

Article

Author: Tang, Shengjia ; Jiao, Guiai ; Wei, Xiangjin ; Chen, Wei ; Shao, Gaoneng ; Tang, Liqun ; Hu, Peisong ; Wang, Yakun ; Hu, Shikai ; Tang, Shaoqing ; Cai, Yicong ; Ahmad, Shakeel ; Xie, Lihong ; Sheng, Zhonghua ; Guo, Naihui ; Li, Qianlong

AbstractAs the source of isoprenoid precursors, the plastidial methylerythritol phosphate (MEP) pathway plays an essential role in plant development. Here, we report a novel rice (Oryza sativa L.) mutant ygl3 (yellow-green leaf3) that exhibits yellow-green leaves and lower photosynthetic efficiency compared to the wild type due to abnormal chloroplast ultrastructure and reduced chlorophyll content. Map-based cloning showed that YGL3, one of the major genes involved in the MEP pathway, encodes 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, which is localized in the thylakoid membrane. A single base substitution in ygl3 plants resulted in lower 4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity and lower contents of isopentenyl diphosphate (IPP) compared to the wild type. The transcript levels of genes involved in the syntheses of chlorophyll and thylakoid membrane proteins were significantly reduced in the ygl3 mutant compared to the wild type. The phytochrome interacting factor-like gene OsPIL11 regulated chlorophyll synthesis during the de-etiolation process by directly binding to the promoter of YGL3 to activate its expression. The findings provides a theoretical basis for understanding the molecular mechanisms by which the MEP pathway regulate chloroplast development in rice.

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