mutase oor Spaans
mutase
en
(biochemistry) An enzyme that catalyzes the shifting of a functional group from one position to another within the same molecule.
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The normal glycolytic pathway generates 1,3-BPG, which may be dephosphorylated by phosphoglycerate kinase (PGK), generating ATP, or it may be shunted into the Luebering-Rapoport pathway, where bisphosphoglycerate mutase catalyzes the transfer of a phosphoryl group from C1 to C2 of 1,3-BPG, giving 2,3-BPG.
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The succinyl CoA molecule formed by the action of methylmalonyl-CoA mutase is metabolized to oxaloacetate.
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The outcome for newborns with complete mutase deficiency is usually poor.
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The mutase deficiencyoccurs mainly in African-Americans.
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What kind of a pericyclic reaction does chorismate mutase catalyze?
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Propose a mechanism for methylmalonyl-CoA mutase, the enzyme that converts methylmalonyl-CoA into succinyl-CoA.
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Glyphosate inhibits the enzyme enolpiruvilchiquimato-phosphate synthase (EPSPS), important to the synthesis of aromatic amino acids; it can also inhibit or repress the action of another two enzymes involved in other steps of amino acid synthesis, that of chloromate mutase and prephrenate hydrathase.
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Methylmalonic Acidemia is a disorder caused by an abnormality of methylmalonyl-CoA mutase or a deficiency of adenosylcobalamin as cofactor.
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Management of newborns with mutase deficiency is similar to management of propionic acidemia.
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It is the major form of phosphoglycerate mutase in fungi, some bacteria, and most animals.
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The defect of methylmalonyl-CoA mutase apoenzyme is the most frequently identified.
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This version of phosphoglycerate mutase is found in plants and some bacteria.
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The methylmalonyl-CoA mutase mechanism begins with the cleavage of the bond between the 5' CH 2- of 5'-deoxyadenosyl and the cobalt, which is in its 3+ oxidation state (III), which produces a 5'-deoxyadenosyl radical and cobalamin in the reduced Co(II) oxidation state.
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Cobalamin is also an essential cofactor for the mutase that converts methylmalonic acid to succinic acid.
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It resembles the family of proteins that include phosphoglycerate mutases and acid phosphatases.
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(A mutase is an enzyme that transfers a group from one position to another.)
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Erythrocytes contain bisphosphoglycerate mutase.
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Accumulation of free 2,3BPG (i.e., 2,3BPG not bound to hemoglobin) inhibits bisphosphoglycerate mutase.
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The catalyzed mutase reaction involves two separate phosphoryl groups and the ending phosphate on the 2-carbon is not the same phosphate removed from the 3-carbon.
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The second type of phosphoglycerate mutase is called cofactor-dependent PGM, or dPGM.
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Methylmalonyl-CoA mutase is one of the few enzymes that require adenosylcobalamin as a cofactor.
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Other names in common use include beta-lysine mutase, and L-beta-lysine 5,6-aminomutase.
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The result was that the hyperthyroidism modulates in vivo 2,3-BPG content in erythrocytes by changes in the expression of phosphoglycerate mutase (PGM) and 2,3-BPG synthase.
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A defect in methylmalonyl-CoA mutase enzyme results in methylmalonic aciduria, a dangerous disorder that causes a lowering of blood pH.
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At least 2 forms of mutase apoenzyme deficiencies have been identified.
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