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In honeybees there are three alleles of cytosolic malate dehydrogenase gene: F, M and S. Allele frequencies are correlated with environmental temperature, suggesting that the alleles have temperature-dependent fitness benefits. We determined the enzyme activity of each allele across a range of temperatures The F and S alleles have higher activity and are less sensitive to high temperatures than the M allele, which loses activity after incubation at temperatures found in the thorax of foraging bees in hot climates. Next, we predicted the protein structure of each allele and used molecular dynamics simulations to investigate their molecular flexibility. The M allozyme is more flexible than the S and F allozymes at 50°C, suggesting a plausible explanation for its loss of activity at high temperatures, and has the greatest structural flexibility at 15°C, suggesting that it can retain some enzyme activity at cooler temperatures. MM bees recovered from 2 h of cold narcosis significantly better than all other genotypes. Combined, these results explain clinal variation in malate dehydrogenase allele frequencies in the honeybee at the molecular level.
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http://dx.doi.org/10.1242/jeb.228239 | DOI Listing |
Biochemistry
September 2025
Department of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.
d-2-Hydroxyglutarate dehydrogenase (D2HGDH) has recently received considerable attention due to the involvement of d-2-hydroxyglutarate in various medical conditions. This enzyme has been reported to diverge in substrate scope depending on whether its source is prokaryotic or eukaryotic. The D2HGDH from , D2HGDH, is of particular interest due to its requirement for survival via the l-serine biosynthesis pathway and its potential use as a therapeutic target against the bacterium.
View Article and Find Full Text PDFFront Plant Sci
August 2025
State Key Laboratory of Tree Genetics and Breeding, Research Institute of Non-Timber Forestry, Chinese Academy of Forestry, Zhengzhou, China.
Introduction: Shikimic acid, as a critical precursor for oseltamivir synthesis in antiviral pharmaceuticals, faces escalating global demand. Although leaves have emerged as a promising natural source of shikimic acid owing to their exceptional content of this valuable compound and substantial biomass production capacity, the molecular mechanisms underlying its biosynthesis and downstream metabolic regulation in leaves remain largely unknown.
Methods: Here, the concentration of shikimic acid in 33 clones were assessed, and 1# (referred as HS) had the highest level.
Anim Reprod Sci
September 2025
College of Animal Science and Technology, Qingdao Agricultural University, Qingdao 266109, China. Electronic address:
Due to the current limitations of boar semen cryopreservation systems, the effective restoration of sperm quality following thawing remains a significant challenge. This study investigates whether post-thaw boar sperm can uptake exogenous long-chain fatty acids (LCFAs) and utilize them for ATP generation, thereby sustaining linear motility and enhancing sperm vitality. Boar semen was diluted in extender solutions supplemented with varying concentrations of a lipid mixture (0, 0.
View Article and Find Full Text PDFBiol Open
September 2025
Institute of Molecular Biosciences, Mahidol University, 25/25 Phuttamonthon 4 Road, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand.
Yeast mitochondrial malate dehydrogenase, Mdh1p, is known to form supramolecular complexes with other TCA cycle and mitochondrial dehydrogenase enzymes, including the aldehyde dehydrogenase, Ald4p. These complexes have been proposed to facilitate NADH channeling. Here, we demonstrate that in cells grown to saturation and stationary phases, the endogenous Mdh1p, expressed without its mitochondrial targeting signal (MTS), stays outside mitochondria, in both a diffuse cytoplasmic distribution as well as localized to distinct puncta.
View Article and Find Full Text PDFPlant Cell Rep
September 2025
Key Laboratory of Germplasm Innovation for the Upper Reaches of the Yangtze River, Ministry of Agriculture and Rural Affairs, Chongqing, 400715, China.
The gene ZmDof08, which underlies the yellow-green leaf mutant phenotype in maize, enhances the activity of key enzymes involved in C photosynthesis, leading to a significant improvement in photosynthetic efficiency. Improving the photosynthetic efficiency of maize to increase its yield has long been a key focus in global agricultural research. Maize possesses a rich resource of leaf color mutants, which serve as valuable materials for studying leaf photosynthesis.
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