Nutrition Guide

Bodybuilding supplements are substances taken by athletes involved in weight training or other sports to aid in the building of lean muscle mass or to cause fat loss. Bodybuilding supplements may also be used to improve sports performance and improve recovery from events and training. One important distinction exists in many weight training groups between supplements and anabolic steroids. There is a common misconception among non-supplement-users that supplementation for muscle-building purposes is the same as steroid use or, at the very least, leads to steroid use.[citation needed] However, this charge is often challenged by supplement users on the grounds that supplements

Meal Replacement Products (MRPs) are either pre-packaged powdered drink mixes or edible bars. Both are consumed in the place of a whole-food meal. Generally MRPs are high in protein, low in fat, have a low to moderate amount of carbohydrates, and contain a wide array of vitamins and minerals. The majority of MRPs use whey protein, calcium caseinate or micellar casein, soy protein, and egg albumin as the protein source. Carbohydrates are typically derived from maltodextrin, oat fiber, brown rice, or wheat flour. Some also contain flax oil powder as a source of essential fatty acids. MRPs can also contain other ingredients

In enzymology, a glutamine N-phenylacetyltransferase (EC 2.3.1.14) is an enzyme that catalyzes the chemical reaction phenylacetyl-CoA + L-glutamine CoA + alpha-N-phenylacetyl-L-glutamine Thus, the two substrates of this enzyme are phenylacetyl-CoA and L-glutamine, whereas its two products are CoA and alpha-N-phenylacetyl-L-glutamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is phenylacetyl-CoA:L-glutamine alpha-N-phenylacetyltransferase. Other names in common use include glutamine phenylacetyltransferase, and phenylacetyl-CoA:L-glutamine N-acetyltransferase. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.

In enzymology, a glutamine-phenylpyruvate transaminase (EC 2.6.1.64) is an enzyme that catalyzes the chemical reaction L-glutamine + phenylpyruvate 2-oxoglutaramate + L-phenylalanine Thus, the two substrates of this enzyme are L-glutamine and phenylpyruvate, whereas its two products are 2-oxoglutaramate and L-phenylalanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:phenylpyruvate aminotransferase. Other names in common use include glutamine transaminase K, and glutamine-phenylpyruvate aminotransferase. It employs one cofactor, pyridoxal phosphate.

In enzymology, a glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction L-glutamine + pyruvate 2-oxoglutaramate + L-alanine Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutaramate and L-alanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:pyruvate aminotransferase. Other names in common use include glutaminase II, L-glutamine transaminase L, and glutamine-oxo-acid transaminase. This enzyme participates in glutamate metabolism. It employs one cofactor, pyridoxal phosphate.

In enzymology, a glutamine N-acyltransferase (EC 2.3.1.68) is an enzyme that catalyzes the chemical reaction acyl-CoA + L-glutamine CoA + N-acyl-L-glutamine Thus, the two substrates of this enzyme are acyl-CoA and L-glutamine, whereas its two products are CoA and N-acyl-L-glutamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:L-glutamine N-acyltransferase.

In enzymology, a glutamine-scyllo-inositol transaminase (EC 2.6.1.50) is an enzyme that catalyzes the chemical reaction L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone 2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol Thus, the two substrates of this enzyme are L-glutamine and 2,4,6/3,5-pentahydroxycyclohexanone, whereas its two products are 2-oxoglutaramate and 1-amino-1-deoxy-scyllo-inositol. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase. Other names in common use include glutamine scyllo-inosose aminotransferase, L-glutamine-keto-scyllo-inositol aminotransferase, glutamine-scyllo-inosose transaminase, and L-glutamine-scyllo-inosose transaminase. It employs one cofactor, pyridoxal phosphate.

In enzymology, a glutamine-scyllo-inositol transaminase (EC 2.6.1.50) is an enzyme that catalyzes the chemical reaction L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone 2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol Thus, the two substrates of this enzyme are L-glutamine and 2,4,6/3,5-pentahydroxycyclohexanone, whereas its two products are 2-oxoglutaramate and 1-amino-1-deoxy-scyllo-inositol. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase. Other names in common use include glutamine scyllo-inosose aminotransferase, L-glutamine-keto-scyllo-inositol aminotransferase, glutamine-scyllo-inosose transaminase, and L-glutamine-scyllo-inosose transaminase. It employs one cofactor, pyridoxal phosphate.

Metabolife was founded in the early 1990's by Michael Ellis, a former police officer on probation for charges relating to his involvement with a methamphetamine lab.[3][4] Ellis and a boyhood friend, Michael Blevins, were arrested in 1989 for producing and distributing methamphetamine. Both Ellis and Blevins cooperated with federal authorities in return for lighter sentences. Following Blevins' release from prison, the two formed Metabolife to market ephedra, an herbal supplement containing compounds chemically related to methamphetamine.[4] Metabolife's ephedra supplement was initially marketed as a bodybuilding supplement, but in 1995 was rebranded as an aid for dieting. The product became highly successful

A gainer is a bodybuilding supplement usually comprised of both high and low glycemic carbohydrates and protein (usually in the form of calcium caseinate, milk and whey protein) and often other nutrients such as certain vitamins and minerals. Gainers are used by bodybuilding and strength athletes, both amateur and professional alike. When performing intensive exercise the stress can cause the release of hormones such as cortisol in order to quickly make available energy to the body. Cortisol forces breakdown of glycogen, protein (muscle) and fat deposits which are used in gluconeogenesis. Gainers seek to combat this effect after (and sometimes during)

A thermogenic is a broad term for any supplement that the manufacturer claims will cause thermogenesis, resulting in an increased metabolic rate, increased body temperature and consequently an increased rate in the burning of body fat. Until recently almost every product found in this supplement category comprised the "ECA stack": ephedrine, caffeine and aspirin. However, on February 6, 2004 the Food and Drug Administration (FDA) banned the sale of ephedra and its alkaloid, ephedrine, for use in weight loss formulas. Several manufacturers replaced the ephedra component of the "ECA" stack with bitter orange or citrus aurantium (containing synephrine) instead of

In addition to being consumed in milk, casein is used in the manufacture of adhesives, binders, protective coatings, plastics (such as for knife handles and knitting needles), fabrics, food additives and many other products. It is commonly used by bodybuilders as a slow-digesting source of amino acids as opposed to the fast-digesting whey protein, and also as an extremely high source of glutamine (post-workout). Another reason it is used in bodybuilding is because of its anti-catabolic effect, meaning that casein consumption inhibits protein breakdown in the body. Casein is frequently found in otherwise nondairy cheese substitutes to improve consistency, especially

In enzymology, a D-glutamyltransferase (EC 2.3.2.1) is an enzyme that catalyzes the chemical reaction L(or D)-glutamine + D-glutamyl-peptide NH3 + 5-glutamyl-D-glutamyl-peptide The 3 substrates of this enzyme are L-glutamine, D-glutamine, and D-glutamyl-peptide, whereas its two products are NH3 and 5-glutamyl-D-glutamyl-peptide. This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is glutamine:D-glutamyl-peptide 5-glutamyltransferase. Other names in common use include D-glutamyl transpeptidase, and D-gamma-glutamyl transpeptidase. This enzyme participates in d-glutamine and d-glutamate metabolism.

In enzymology, a glutamine-fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) is an enzyme that catalyzes the chemical reaction L-glutamine + D-fructose 6-phosphate L-glutamate + D-glucosamine 6-phosphate Thus, the two substrates of this enzyme are L-glutamine and D-fructose 6-phosphate, whereas its two products are L-glutamate and D-glucosamine 6-phosphate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:D-fructose-6-phosphate isomerase (deaminating). Other names in common use include hexosephosphate aminotransferase, glucosamine-6-phosphate isomerase (glutamine-forming), glutamine-fructose-6-phosphate transaminase (isomerizing), D-fructose-6-phosphate amidotransferase, glucosaminephosphate isomerase, glucosamine 6-phosphate synthase, and GlcN6P synthase. This enzyme participates in glutamate metabolism and

In enzymology, a protein-glutamine glutaminase (EC 3.5.1.44) is an enzyme that catalyzes the chemical reaction protein L-glutamine + H2O protein L-glutamate + NH3 Thus, the two substrates of this enzyme are protein L-glutamine and H2O, whereas its two products are protein L-glutamate and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is protein-L-glutamine amidohydrolase. Other names in common use include peptidoglutaminase II, glutaminyl-peptide glutaminase, destabilase, and peptidylglutaminase II.

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