endurance training will have improved endurance performance on oxidative enzymes.
endurance training will have improved endurance performance on oxidative enzymes.
what effect will endurance training have on oxidative enzymes?
improved endurance performance
long-term endurance training induces many physiological adaptations both centrally and peripherally mediated. central cardiovascular adaptations include decreased heart rate, increased stroke volume of the heart, increased blood plasma, without any major changes in red blood cell count, which reduces blood viscosity and increased cardiac output as well as total mitochondrial volume in the muscle fibers used in the training (i.e. the thigh muscles in runners will have more mitochondria than the thigh muscles of swimmers). mitochondria increase in both number and size and there are similar increases in myoglobin and oxidative enzymes. adaptations of the peripheral include capillarization, that is an increase in the surface area that both the venous and arterial capillaries supply. this also allows for increased heat dissipation during strenuous exercise. the muscles heighten their glycogen and fat storing capabilities in endurance athletes in order to increase the length in time in which they can perform work. endurance training primarily work the slow twitch (type 1) fibers and develop such fibers in their efficiency and resistance to fatigue. catabolism also improves increasing the athletes capacity to use fat and glycogen stores as an energy source. these metabolic processes are known as glycogenolysis, glycolysis and lipolysis. there is higher efficiency in oxygen transport and distribution. in recent years it has been recognized that oxidative enzymes such as succinate dehydrogenase (sdh) that enable mitochondria to break down nutrients to form atp increase by 2.5 times in well trained endurance athletes in addition to sdh, myoglobin increases by 75-80% in well trained endurance athletes.
endurance training
in lignan biosynthesis, oxidative enzymes perform proton coupled electron transfer to remove a hydrogen atom from monolignols, forming a radical intermediate. these intermediates then couple in a radical termination reaction to form one of a variety of dimers, known as lignans. "in vitro" reactions of coniferyl alcohol (a common monolignol) in the presence of oxidative enzymes produce a wide variety of different dimers at varying concentrations. when dirigent protein from "forsythia intermedia" is present, production of (+)-pinoresinol is greatly enriched, and other products are far less abundant. because this enrichment is so pronounced, the enzyme is hypothesized to produce (+)-pinoresinol exclusively, and to compete with the non-protein-mediated coupling reaction, which produces a heterologous mix of products. this has been confirmed by analyzing the various mixtures produced with different concentrations of dirigent proteins present. the mechanism by which this stereoselectivity is achieved is not well understood at this time. however, since no reaction proceeds in the absence of oxidative enzymes, dirigent protein does not itself appear to catalyze the oxidation of coniferyl alcohol to form radicals.
dirigent protein