SEARCH · PubMed Health
Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.
Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
The growth requirement or growth-promoting effect of biotin-vitamers on bacteria and yeasts was investigated. Biotin, dethiobiotin and biocytin (N-e-biotinyl-L-lysine) were shown to be required for growth in a number of bacteria and yeasts. The biological activity of dethiobiotin was relatively higher than that of biotin, but was negative for lactic acid bacteria. Biocytin had high activity for Bacillus subtilis (natto), Debaryomyces japonicus and Hansenula capsulata. The biotin activity of 7-keto-8-aminopelargonic and 7,8-diaminopelargonic acids was low or negligible for bacteria but relatively high for yeasts such as the genera of Endomyces, Endomycopsis and Saccharomyces. Pimelic, pelargonic and pelargonylhydroxamic acids had no growth requirement for or growth-promoting effect on any of the bacteria or yeasts tested.
A yeast capable of utilizing cyclohexanecarboxylic acid as sole carbon and energy source, strain KUY-6A, was isolated from soil by enrichment cultures. Taxonomical studies indicated that strain KUY-6A was Trichosporon cutaneum. Strain KUY-6A grew on a number of carboxylic acids. Among the cyclic compounds tested, cyclohexanecarboxylic acid was the best substrate. Cyclopentanecarboxylic acid, cycloheptanecarboxylic acid, cyclopentanone, cyclohexanone, and cyclopentanol also supported growth. In addition, the organism used the monocarboxylic acids, butyric, valeric, and caproic; the dicarboxylic acids succinic, glutaric, adipic, pimelic, and suberic; and the aromatic acids, benzoic and o-, m-, and p-hydroxybenzoic. The yeast did not require any vitamins for growth, although thiamine gave slight stimulation. The cell dry weight yield was 0.75 g from 1 g cyclohexanecarboxylic acid used.
The blocking action of alpha-polypeptides from the venoms of elapid snakes (Bungarus multicinctus and Naja naja siamensis) was studied on leech dorsal muscle. It was shown that these neurotoxins failed to inhibit the responses to mononitrogen cholinomimetics (acetylcholine, nicotine, carbamylcholine, etc.). The capacity of neurotoxins to inhibit the responses to the bisquaternary cholinommimetics depended upon the length of the molecule. The neurotoxins were active against the "shorter" cholinomimetics, such as decamethonium, and bischolinic esters of malonic, succinic and glutaric acids. The "longer" cholinomimetics (bischolinic esters of adipinic, pimelic, suberic, azelaic, sebacic acids retained their full activity after the treatment of leech dorsal muscle by neurotoxins. Possible explanations of the selective action of neurotoxins are discussed.
A number of porphyrin derivatives have been found to inhibit yeast glyoxalase I (EC 4.4.1.5) at 25 degrees C, including haemin, protoporphyrin IX, coproporphyrin III, haematoporphyrin, deuteroporphyrin as well as meso-(tetrasubstituted) porphines. Bilirubin and chlorophyllin were also inhibitory, but not cobalamin, adipic, pimelic or suberic acids. Whilst the Ki value for linear competitive inhibition by meso-tetra(4-methylpyridyl)porphine was pH-dependent, analogous Ki values for meso-tetra(4-carboxyphenyl)- and meso-tetra(4-sulphonatophenyl)porphines followed the Henderson-Hasselbalch equation with pKapp values of 7.10 and 6.50, respectively. Protoporphyrin showed similar behaviour (pKapp 7.06) with a deviation at lower pH. The haemin pH profile for Ki showed a maximum at approx. pH 6.5. The redox reaction between haemin and glutathione did not interfere in the inhibition studies. The Ki value for S-(p-bromobenzyl)glutathione was pH-independent. A detailed analysis of porphyrin binding modes was undertaken.
L-Kynurenine aminotransferase [L-kynurenine:2-oxoglutarate aminotransferase (cyclizing), EC 2.6.1.7] has been purified to homogeneity and crystallized from cell-free extracts of a yeast, Hansenula schneggii, grown in a medium containing L-tryptophan as an inducer. The enzyme has a molecular weight of about 100,000 and consists of two subunits identical in molecular weight (52,000). The enzyme exhibits absorption maxima at 280, 335, and 430 nm, and contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme. The enzyme-bound pyridoxal 5'-phosphate shows negative circular dichroic extrema, in contrast with other pyridoxal 5'-phosphate acting on L-amino acids. In addition to L-kynurenine and alpha-ketoglutarate, which are the most preferred substrates, a large number of L-amino acids and alpha-keto acids can serve as substrates; the extremely broad substrate specificity is the most characteristic feature of this yeast enzyme. The enzyme activity is significantly affected by both carbonyl and sulfhydryl reagents. Certain dicarboxylic acids such as adipate and pimelate act as competitive inhibitors. Addition of various substrate amino acids to the culture medium results in the inductive formation of aminotransferases which are immunochemically indistinguishable from L-kynurenine aminotransferase.
The biochemistry of the 13 steps involved in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to the coenzymes coenzyme B (7-mercapto heptanoylthreonine phosphate) and biotin, has been established in Methanosarcina thermophila. These series of reactions begin with the condensation of alpha-ketoglutarate and acetylCoA to form trans-homoaconitate. The trans-homoaconitate is then hydrated and dehydrated to cis-homoaconitate with (S)-homocitrate serving as an intermediate. Rehydration of the cis-homoaconitate produces (-)-threo-isohomocitrate [(2R,3S)-1-hydroxy-1,2, 4-butanetricarboxylic acid], which undergoes a NADP+-dependent oxidative decarboxylation to produce alpha-ketoadipate. The resulting alpha-ketoadipate then undergoes two consecutive sets of alpha-ketoacid chain elongation reactions to produce alpha-ketosuberate. In each of these sets of reactions, it has been shown that the homologues of cis-homoaconitate, homocitrate, and (-)-threo-isohomocitrate serve as intermediates. The protein product of the Methanococcus jannaschii MJ0503 gene aksA (AksA) was found to catalyze the condensation of alpha-ketoglutarate and acetylCoA to form trans-homoaconitate. This gene product also catalyzed the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologues of (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2, 6-hexanetricarboxylic acid. The alpha-ketosuberate resulting from this series of reactions then undergoes a nonoxidative decarboxylation to form 7-oxoheptanoic acid, a precursor to coenzyme B, and an oxidative decarboxylation to form pimelate, the precursor to biotin. Of the 13 intermediates in this pathway, eight have not previously been reported as occurring in biological systems.