Content of tree and bound thiamine pyrophosphate (TPP) was measured by means of gel filtration and equilibrium dialysis procedures in mitochondria of normal rats, the rats under conditions of alimentary B1 avitaminosis and loading with thiamine. The content of protein-bound TPP was stable and equal to 20% of its total level in the mitochondria of control rats and in the rats loaded with thiamine. The content of free form of TPP was decreased in B1 avitaminosis; a severe form of the avitaminosis was accompanied by a decrease in content of the bound form. Concentration of the free form of TPP did not increase if the organism of the rats was loaded with thiamine. These data suggest existence of specific systems controlling the vitamin uptake in mitochondria. The active transport of thiamine across the mitochondrial membranes is considered as the most important process. Administration of the high doses of the vitamin led only to an increase in the non-coenzymatic form of the vitamin, indicating the absence of thiamine pyrophosphokinase in rat liver mitochondria. A possible mechanism of TPP transport in mitochondria is discussed.
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Biochemistry
December 2024
Department of Life Science, Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, Japan.
The RhiE and RhiF proteins work together as RhiEF and function as a thiamine pyrophosphate (TPP)-dependent phosphonopyruvate decarboxylase to produce phosphonoacetaldehyde in the rhizocticin biosynthesis pathway. In this study, we determined the crystal structure of the RhiEF complexed with TPP and Mg. RhiEF forms a dimer of heterodimers, and the cofactor TPP is bound at the heterotetrameric subunit interface.
View Article and Find Full Text PDFAm J Clin Nutr
November 2024
Noguchi Memorial Institute for Medical Research, University of Ghana, Legon, Ghana. Electronic address:
Background: Gaps persist in the data on diets and on the validity of dietary assessment methods in youth in low-income and middle-income countries (LMICs) due to costs constraints. Although computer vision-assisted dietary assessment tools have been proposed, limited evidence exists on their validity in LMICs.
Objectives: This study aimed to validate FRANI (Food Recognition Assistance and Nudging Insights), a mobile phone application with computer vision-assisted dietary assessment, against weighed records (WRs) and compare with 24-h recalls (24HR), in female youth in Ghana.
Nano Lett
September 2024
State Key Laboratory of Analytical Chemistry for Life Sciences, School of Chemistry and Chemical Engineering, Nanjing University, 210023 Nanjing, China.
Vitamin Bs, a group of water-soluble compounds, are essential nutrients for almost all living organisms. However, due to their structural heterogeneity, rapid and simultaneous analysis of multiple vitamin Bs is still challenging. In this paper, it is discovered that a hetero-octameric porin A (MspA) nanopore containing a sole nickel ion-bound nitrilotriacetic acid (NTA-Ni) adapter at its pore constriction is suitable for the simultaneous sensing of different vitamin Bs, including vitamin B1 (thiamine), vitamin B3 (nicotinic acid and nicotinamide), vitamin B5 (pantothenic acid), and vitamin B6 (pyridoxine, pyridoxal, and pyridoxamine).
View Article and Find Full Text PDFChembiochem
December 2024
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205, United States.
1-Deoxy-d-xylulose 5-phosphate synthase (DXPS) catalyzes the thiamin diphosphate (ThDP)-dependent formation of DXP from pyruvate (donor substrate) and d-glyceraldehyde 3-phosphate (d-GAP, acceptor substrate) in bacterial central metabolism. DXPS uses a ligand-gated mechanism in which binding of a small molecule "trigger" activates the first enzyme-bound intermediate, C2α-lactylThDP (LThDP), to form the reactive carbanion via LThDP decarboxylation. d-GAP is the natural acceptor substrate for DXPS and also serves a role as a trigger to induce LThDP decarboxylation in the gated step.
View Article and Find Full Text PDFCommun Chem
July 2024
eBERlight and Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, USA.
2-Hydroxyacyl-CoA lyase/synthase (HACL/S) is a thiamine diphosphate (ThDP)-dependent versatile enzyme originally discovered in the mammalian α-oxidation pathway. HACL/S natively cleaves 2-hydroxyacyl-CoAs and, in its reverse direction, condenses formyl-CoA with aldehydes or ketones. The one-carbon elongation biochemistry based on HACL/S has enabled the use of molecules derived from greenhouse gases as biomanufacturing feedstocks.
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