Biological Studies on Thiamine Related Compound (IV)
نویسندگان
چکیده
منابع مشابه
Studies on Thiamine Analocues
Several analogues of thiamine’ are known to compete with the vitamin when administered to animals. Thus, Woolley and White (1) have observed that pyrithiamine caused the manifestation of typical thiamine deficiency symptoms, which could be competitively overcome by the vitamin. The antivitamin effect of oxythiamine in mice has been reported by Soodak and Cerecedo (2). Cerecedo et al. (3, 4), co...
متن کاملStudies on thiamine diphosphate-dependent enzymes.
The 3-deaza analogue of TPP (thiamine diphosphate), a close mimic of the ylid intermediate, has been synthesized and is an extremely potent inhibitor of a variety of TPP-dependent enzymes, binding much more tightly than TPP itself. Results using deazaTPP complexed with the E1 subunit of PDH (pyruvate dehydrogenase) have led to a novel proposal about the mechanism of this enzyme. The 2-substitut...
متن کاملDesign, Synthesis and Biological Evaluation of Brain-Targeted Thiamine Disulfide Prodrugs of Ampakine Compound LCX001.
Ampakine compounds have been shown to reverse opiate-induced respiratory depression by activation of amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) glutamate receptors. However, their pharmacological exploitations are hindered by low blood-brain barrier (BBB) permeability and limited brain distribution. Here, we explored whether thiamine disulfide prodrugs with the ability of "lock-i...
متن کاملThiamine pyrophosphate riboswitches are targets for the antimicrobial compound pyrithiamine.
Thiamine metabolism genes are regulated in numerous bacteria by a riboswitch class that binds the coenzyme thiamine pyrophosphate (TPP). We demonstrate that the antimicrobial action of the thiamine analog pyrithiamine (PT) is mediated by interaction with TPP riboswitches in bacteria and fungi. For example, pyrithiamine pyrophosphate (PTPP) binds the TPP riboswitch controlling the tenA operon in...
متن کاملStudies on the Nature of the Binding of Thiamine Pyrophosphate
The binding of thiamine pyrophosphate (TPP) to several enzymes has been determined by measuring cofactordependent activity after passage of each enzyme through a column of Sephadex G-25 to remove non-protein-bound cofactors. TPP was found to be bound irreversibly to yeast and Zymomonas pyruvate decarboxylases, Aerobacter (Yacetolactate synthetase, and Escherichia glyoxylate carboligase. Cofacto...
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ژورنال
عنوان ژورنال: The Japanese Journal of Nutrition and Dietetics
سال: 1961
ISSN: 1883-7921,0021-5147
DOI: 10.5264/eiyogakuzashi.19.133