Ask about this productRelated genes to: BDH2 antibody
- Gene:
- BDH2 NIH gene
- Name:
- 3-hydroxybutyrate dehydrogenase 2
- Previous symbol:
- DHRS6
- Synonyms:
- UCPA-OR, FLJ13261, UNQ6308, PRO20933, SDR15C1
- Chromosome:
- 4q24
- Locus Type:
- gene with protein product
- Date approved:
- 2005-11-22
- Date modifiied:
- 2016-12-12
Related products to: BDH2 antibody
Related articles to: BDH2 antibody
- Epidemiological studies suggest associations of asthma with the psychosis spectrum (psychotic experiences, bipolar disorder, schizophrenia), but the mechanisms underlying these associations remain unclear. - Source: PubMed
Publication date: 2026/08/06
Dardani ChristinaRobinson Jamie WHavdahl AlexandraDarrous LizaJones Hannah JZammit StanSullivan Sarah ARai DheerajStergiakouli EvieZhu ZhaozhongLiang LimingNava George WGardner ReneeGrove JakobRichardson Tom GSmith George DaveyDodd James WHemani GibranGaunt Tom RKhandaker Golam M - Camphor is a key quality determinant of lavender oil. Bornyl dehydrogenase (BDH) catalyzes the final camphor biosynthesis step, yet its gene family and mechanism in lavender remain uncharacterized. We phylogenetically classified 154 short-chain dehydrogenase/reductase () genes into six clades and screened 17 genes. Integrated transcriptomic and metabolomic analyses revealed that camphor biosynthesis primarily occurs via the plastidic 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway, with coordinated expression of geranyl diphosphate synthase (), bornyl diphosphate synthases (), bornyl-diphosphate diphosphatase (), and genes. Most biosynthetic genes, especially and , were significantly upregulated in "Xinxun 4", correlating with its highest camphor content. Subcellular localization showed BDH1 resides in the cytoplasm, suggesting plastid-cytoplasm collaboration. In vitro assays demonstrated that BDH1 and BDH2 both oxidize (+)- and (-)-borneol to camphor. Molecular dynamics simulations revealed that BDH1's active site exhibits conformational flexibility, accommodating both enantiomers with similar binding affinities, which was confirmed by enzyme kinetics. Asn90 was identified as a key catalytic residue. These findings reveal BDH family expansion, coordinated gene expression driving camphor accumulation, and BDH1's catalytic flexibility, offering key genetic resources and mechanistic insights for optimizing lavender camphor content via metabolic engineering and molecular breeding. - Source: PubMed
Publication date: 2026/06/07
Zeng YulingNie JingLan HaiyanZhang YichaoDai YufangCao XiaojieZhang LiangHu Jianjian - Adaptation is one of the key processes of animal domestication, environmental pressures will leave footprints in the genome. Geese are widely distributed across multiple geographical conditions with distinct adaptations. However, few reports have focused on the environmental adaptability of geese. Moreover, the key environmental drivers that trigger local adaptation and its genetic mechanisms are still unknown. To this end, 35 agro-climatic variables of 257 geese from 14 Chinese breeds were obtained, the key environmental drivers and its genetic mechanism were elucidated by combining the genome data. - Source: PubMed
Publication date: 2026/05/30
Zhou XiaoliXia JunliangChen WeidingZou JiajiaChen JiahuiZhang Xiquan - Emerging evidence has demonstrated the additional therapeutic benefits of ticagrelor in acute coronary syndrome (ACS) patients with diabetes. However, the underlying mechanisms of this association remain elusive. Mendelian randomization (MR) analysis using genome-wide association study (GWAS) data on ticagrelor, plasma proteomics and type 2 diabetes was employed to identify causal mediator proteins. RNA sequencing (RNA-seq) of ticagrelor-treated HepG2 cells revealed the molecular pathways regulating glucose metabolism. Genetically proxied ticagrelor was significantly associated with a reduced risk of diabetes (OR = 0.859, 95% CI: 0.783-0.934, P = 7.98E-05), and 24.41% of this effect was mediated by upregulation of BDH2 protein. In vitro experiments confirmed the enhanced effect of ticagrelor on glucose consumption. Transcriptome analysis revealed that mitochondrial respiratory chain transfer and oxidative phosphorylation (OXPHOS) were significantly enriched, and genes related to ATP biosynthesis were significantly upregulated. These findings highlight the non-platelet function of ticagrelor in maintaining glucose homeostasis, providing insights into potential drug repurposing in the future. - Source: PubMed
Publication date: 2026/05/20
Xie ZhipengMa HeshuoLiu YingjianLai Weihua - Cells possess intricate metabolic networks comprising hundreds of enzymes. Despite extensive research, many of these enzymes remain uncharacterized. Identifying the function of these enzymes is crucial for advancing our understanding of cellular metabolism. However, multiple enzymes are not active in standard conditions, making them challenging to study. To overcome this challenge, we created a pipeline to track the upregulation of enzymes at the protein level during diverse growth conditions, suggesting a requirement for their activity in these conditions. To do this, we assembled a collection of ∼180 yeast strains, each containing an uncharacterized putative enzyme fused to a fluorophore and under the regulation of its own promoter. By subjecting the collection to 42 diverse environments, we identified the biologically relevant conditions for the upregulation of 16 proteins. We focused on one such putative alcohol dehydrogenase, Bdh2, whose expression was upregulated during nutrient-limited conditions, and functionally characterized it. More broadly, our discovery pipeline lays the foundation for uncovering new stress-induced enzymes. This has implications for the cell biology of metabolism and biotechnology. - Source: PubMed
Publication date: 2026/06/12
Edilbi DunyaValenti RosarioDubreuil BenjaminAsraf YeynitPeleg YoavAlbeck ShiraMalitsky SergeyItkin MaximSchuldiner Maya