mutase


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Related to mutase: enolase

mu·tase

 (myo͞o′tās, -tāz)
n.
An enzyme that catalyzes the shifting of a chemical group from one position to another within the same molecule.

[Latin mūtāre, to change, move; see mutate + -ase.]

mutase

(ˈmʌteɪz)
n
(Biochemistry) biochem an enzyme which catalyzes the transfer of a functional group between two positions within the same molecule
References in periodicals archive ?
This is a global, multi-center, non-interventional study for patients with confirmed diagnosis of MMA due to methylmalonyl-CoA mutase (MUT) deficiency or PA and is designed to identify and correlate clinical and biomarker endpoints for these disorders.
This reaction requires the involvement of three enzymes: propionyl-CoA-carboxylase, methylmalonyl-CoA-racemase and methylmalonyl-CoA mutase (Voet et al., 2008).
The level of methylmalonic acid in the blood and urine and the level of homocysteine in the plasma increase due to the reduced activity of the methylmalonyl-CoA mutase enzyme and methionine synthase enzymes in vitamin B12 deficiency.12 The levels of plasma homocysteine and methylmalonic acid in the urine and the levels of total, direct, and indirect bilirubin were compared, and once again, there was no significant difference.
Keywords: Methylmalonic aciduria, Methylmalonyl-CoA mutase deficiency, Cobalamin related remethylation disorders, Vitamin B 12 deficiency, Pakistan.
Several enzymes are involved in the incorporation of these substrates in the gluconeogenesis pathway [3]: lactate dehydrogenase (LDH) for lactate; glycerol kinase (GK) and glycerol-3-phosphate dehydrogenase (GPD) for glycerol; and acyl-CoA synthetase short-chain family member 3 (ACSS3), propionyl-CoA carboxylase (PCC), methylmalonyl-CoA epimerase (MCEE), and methylmalonyl-CoA mutase (MUT) for propionate.
Downstream of the necrosome are two splice variants of phosphoglycerate mutase family member 5 (PGAM5), PGAM5S and PGAM5L.
gpmA and eno encode phosphoglycerate mutase and enolase, respectively, which have been known to participate in substrate level phosphorylation as glycolytic enzymes in carbon metabolism.
Other subtype B genes that have become pseudogenes in subtype A specimens and are associated with metabolic pathways are those encoding a haloacid dehalogenase (LBJ_RS17075) and a methylmalonyl-CoA mutase (LBJ_RS11290), although these genes appear to have putative paralogs with similar function in the genome.
The data, published online in the journal Cell Reports, demonstrate that intravenous administration of an mRNA therapeutic encoding for human methylmalonyl-CoA mutase, the enzyme most frequently mutated in MMA, enabled liver expression of MUT in MMA mouse models, leading to a significant reduction in methylmalonic acid, a substantial improvement in weight gain, and the complete survival of the full cohort of treated mice versus control group.
The target enzyme, cofactor-independent phosphoglycerate mutase (iPGM), is found in both parasites and bacteria.
Nevertheless, PEP may promote the production of pyruvate independent of PKM2 activity through serving as a phosphodonor for phosphoglycerate mutase 1 (PGAM1) [66].
Vitamin B12 is involved in both methylmalonyl-CoA mutase and methionine synthase intracellular pathways.