Analyze Diet

Topic:Yeast

Yeast, a type of fungus, is often incorporated into equine nutrition and management practices due to its potential effects on digestive health and feed efficiency in horses. Yeast supplements, particularly those containing Saccharomyces cerevisiae, are studied for their ability to influence gut microbiota, enhance fiber digestion, and stabilize hindgut pH levels. These properties may contribute to improved nutrient absorption and overall gastrointestinal function. Research also explores the impact of yeast on equine immune function and stress response. This page compiles peer-reviewed research studies and scholarly articles that investigate the effects, mechanisms, and applications of yeast supplementation in equine health and nutrition.
Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c.
Science (New York, N.Y.)    December 11, 1992   Volume 258, Issue 5089 1748-1755 doi: 10.1126/science.1334573
Pelletier H, Kraut J.The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c was determined at 2.3 A resolution. This structure reveals a possible electron transfer pathway unlike any previously proposed for this extensively studied redox pair. The shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191, the indole ring of which is perpendicular to, and in van der Waals contact with, the peroxidase heme. The crystal structure at 2.8 A of a complex between yeast cytochrome c pe...
Flexibility and folding of phosphoglycerate kinase.
Biochimie    June 1, 1990   Volume 72, Issue 6-7 417-429 doi: 10.1016/0300-9084(90)90066-p
Yon JM, Desmadril M, Betton JM, Minard P, Ballery N, Missiakas D, Gaillard-Miran S, Perahia D, Mouawad L.Flexibility and folding of phosphoglycerate kinase, a two-domain monomeric enzyme, have been studied using a wide variety of methods including theoretical approaches. Mutants of yeast phosphoglycerate kinase have been prepared in order to introduce cysteinyl residues as local probes throughout the molecule without perturbating significantly the structural or the functional properties of the enzyme. The apparent reactivity of a unique cysteine in each mutant has been used to study the flexibility of PGK. The regions of larger mobility have been found around residue 183 on segment beta F in the ...
Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: a fluorescence quenching study on the ionic strength dependence of the interaction.
Archives of biochemistry and biophysics    November 1, 1987   Volume 258, Issue 2 621-629 doi: 10.1016/0003-9861(87)90385-7
Vitello LB, Erman JE.The binding of horse heart cytochrome c to yeast cytochrome c peroxidase in which the heme group was replaced by protoporphyrin IX was determined by a fluorescence quenching technique. The association between ferricytochrome c and cytochrome c peroxidase was investigated at pH 6.0 in cacodylate/KNO3 buffers. Ionic strength was varied between 3.5 mM and 1.0 M. No binding occurs at 1.0 M ionic strength although there was a substantial decrease in fluorescence intensity due to the inner filter effect. After correcting for the inner filter effect, significant quenching of porphyrin cytochrome c pe...
A comparative study of the effect of triazine herbicides on alcohol dehydrogenases isolated from various sources.
Environmental research    April 1, 1983   Volume 30, Issue 2 389-392 doi: 10.1016/0013-9351(83)90224-4
Leblová S, Galociová J, Cerovská N.The studied herbicides (terbutylazine, simazine) inhibit the activity of plant, animal, and yeast alcohol dehydrogenases. The inhibition constant Ki for alcohol dehydrogenase (ADH) isolated from peas and bakers' yeast equals approximately 10(-4) M, and that for ADH isolated from horse liver is of the order of 10(-5) M. The character of inhibition for all the herbicides studied for the reaction catalyzed by pea, liver, and yeast ADH is always noncompetitive toward ethanol and competitive with respect to NAD. The inhibition constants for the enzyme isolated from peas are pH independent. The inte...
Alcohol dehydrogenase from Leuconostoc mesenteroides: molecular properties in comparison with the yeast and horse liver enzyme.
The International journal of biochemistry    January 1, 1981   Volume 13, Issue 12 1215-1224 doi: 10.1016/0020-711x(81)90067-7
Schneider-Bernlöhr H, Fiedler H, Gerber M, Weber C, Zeppezauer M.No abstract available
Alkaline isomerization of horse and yeast cytochromes C. Spectrophotometric and circular dichroism studies.
International journal of peptide and protein research    November 1, 1978   Volume 12, Issue 5 233-236 
Looze Y, Polastro E, Deconinck M, Leonis J.Spectrophotometric studies of the alkaline isomerization of horse heart and yeast cytochrome c show that the haemoproteins from Saccharomyces cerevisiae differ significantly from the mammalian cytochrome c. Apparent pKa values of 8.41, 8.40 and 8.73 for isol-1-(the methylated and unmethylated forms) and iso-2-cytochrome c respectively, from baker's yeast were determined and compared with the value of 9.40 found for horse heart cytochrome c. The transitions, measured by observing the decrease of the absorbance at 695 nm as the pH increases, have been found to strictly parallel the decrease in a...
[The incidence and significance of yeasts on equine genital mucosas].
DTW. Deutsche tierarztliche Wochenschrift    October 5, 1978   Volume 85, Issue 10 389-393 
Sonnenschein B, Weiss R, Bringewatt W.No abstract available
Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase.
The Journal of biological chemistry    February 10, 1977   Volume 252, Issue 3 919-926 
Kang CH, Ferguson-Miller S, Margoliash E.1. The steady state kinetics for the oxidation of ferrocytochrome c by yeast cytochrome c peroxidase are biphasic under most conditions. The same biphasic kinetics were observed for yeast iso-1, yeast iso-2, horse, tuna, and cicada cytochromes c. On changing ionic strength, buffer anions, and pH, the apparent Km values for the initial phase (Km1) varied relatively little while the corresponding apparent maximal velocities varied over a much larger range. 2. The highest apparent Vmax1 for horse cytochrome c is attained at relatively low pH (congruent to 6.0) and low ionic strength (congruent to...
Horse liver alcohol dehydrogenase. A study of the essential lysine residue.
The Biochemical journal    September 1, 1975   Volume 149, Issue 3 627-635 doi: 10.1042/bj1490627
Chen SS, Engel PC.1. The inactivation of horse liver alcohol dehydrogenase by pyridoxal 5'-phosphate in phosphate buffer, pH8, at 10 degrees C was investigated. Activity declines to a minimum value determined by the pyridoxal 5'-phosphate concentration. The maximum inactivation in a single treatment is 75%. This limit appears to be set by the ratio of the first-order rate constants for interconversion of inactive covalently modified enzyme and a readily dissociable non-covalent enzyme-modifier complex. 2. Reactivation was virtually complete on 150-fold dilution: first-order analysis yielded an estimate of the r...
Methanol activity o alcohol dehydrogenases from human liver, horse liver, and yeast.
Archives of biochemistry and biophysics    September 1, 1970   Volume 140, Issue 1 52-59 doi: 10.1016/0003-9861(70)90009-3
Mani JC, Pietruszko R, Theorell H.No abstract available
CANDIDA SILVAE SP.N., A YEAST ISOLATED FROM HUMANS AND HORSES.
Antonie van Leeuwenhoek    January 1, 1963   Volume 29 261-264 doi: 10.1007/BF02046067
VIDAL-LEIRIA M, VANUDEN N.No abstract available
Treatment of tropical ulcers in equines with yeast.
The Veterinary record    June 2, 1951   Volume 63, Issue 22 377-378 doi: 10.1136/vr.63.22.377
CALLEAR JF.No abstract available