ArticlePlant signaling & behavior2015
The amino-terminal conserved domain of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase is critical for its function in oxygen-evolving photosynthetic organisms.
Article in Plant signaling & behavior, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 12 citations in OpenAlex.
- The ubiquitin receptor StDA1 negatively regulates aurantio-obtusin biosynthesis by mediating the degradation of the StHDR1 protein in Senna tora seeds.Communications biology · 2026Article
- NbHDR, A Host Protein Involved in the MEP Pathway, Interacts With Bamboo Mosaic Virus Replicase and Enhances Viral Accumulation.Molecular plant pathology · 2025Article
- HDR, the last enzyme in the MEP pathway, differently regulates isoprenoid biosynthesis in two woody plants.Plant physiology · 2023Article
- Biosynthetic pathways of triterpenoids and strategies to improve their Biosynthetic Efficiency.Plant growth regulation · 2022Review
- Differential Regulation of an OsIspH1, the Functional 4-Hydroxy-3-Methylbut-2-Enyl Diphosphate Reductase, for Photosynthetic Pigment Biosynthesis in Rice Leaves and Seeds.Frontiers in plant science · 2022Article
- Transcriptome Sequencing Analysis Reveals a Difference in Monoterpene Biosynthesis between ScentedFrontiers in plant science · 2017Article
- Overexpression and Suppression ofFrontiers in plant science · 2017Article
- Structure and Function of Four Classes of the 4Fe-4S Protein, IspH.Biochemistry · 2016Article
- IspH-RPS1 and IspH-UbiA: "Rosetta Stone" Proteins.Chemical science · 2015Article
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2 authors at 1 institution in 1 country.
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Abstract
4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), also known as isoprenoid synthesis H (IspH) or lysis-tolerant B (LytB), catalyzes the last step of the methylerythritol phosphate pathway to synthesize isopentenyl diphosphate and dimethylallyl diphosphate. The structure and reaction mechanism of IspH have been actively investigated in Escherichia coli but little is known in plants. Compared with the bacterial IspH, cyanobacterial and plant HDRs all contain an extra N-terminal conserved domain (NCD) that is essential for their function. Tyr72 in the NCD and several plant-specific residues around the central active site are critical for Arabidopsis HDR function. These results suggest that the structure and reaction mechanism of HDR/IspH may be different between plants and bacteria. The E. coli IspH is an iron-sulfur protein that is sensitive to oxygen. It is possible that the cyanobacterial HDR may independently evolve from the common ancestor of prokaryotes to obtain the NCD, which may protect the enzyme from high concentration of oxygen during photosynthesis.
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