Results 151 to 160 of about 80,661 (193)
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Methylmalonyl CoA mutase—A radiochromatographic assay
Clinica Chimica Acta, 1972Abstract A new assay for leucocyte methylmalonyl CoA mutase is described. The [14C]-succinate produced in this assay is separated from the substrate [14C]methylmalonate by semi-preparative gas chromatography. The efficiency of this separation has allowed a linear assay of enzyme activity to be developed.
P A, Goodey, D, Gompertz
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Assay of Methylmalonyl CoA Mutase With High-Performance Liquid Chromatography
Clinica Chimica Acta, 1989An assay for methylmalonyl CoA mutase activity is described. Succinyl CoA produced in this method is separated from the substrate, methylmalonyl CoA, by reverse-phase high-performance liquid chromatography and is quantified. This method is useful to differentiate mutase apoenzyme deficiency (mut0, mut-) and the defect in deoxyadenosylcobalamin ...
Kuniaki Narisawa, Keiya Tada, K Narisawa
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Is there methylmalonyl CoA mutase in Aspergillus nidulans?
Biochemical and Biophysical Research Communications, 1991In most animal species and many prokaryotes, methylmalonyl CoA mutase catalyzes isomerization between methylmalonyl CoA and succinyl CoA using adenosylcobalamin as a cofactor. We describe the absence of this enzyme in Aspergillus nidulans based on the absence of enzyme activity in vitro and the failure to metabolize methylmalonate or grow in media ...
F D, Ledley +3 more
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Methylmalonyl-CoA mutase encoding gene of Sinorhizobium meliloti
Gene, 1999A cluster of genes on megaplasmid pRmeSU47b, bhbA-D, is required for growth on the polyhydroxyalkanoate degradation pathway intermediates 3-hydroxybutyrate and acetoacetate as sole carbon source. DNA sequence analysis of the bhbA gene indicated that it encoded a protein of 712 amino acids (aa) (78kDa) which appeared to be a homodimeric methylmalonyl ...
T C, Charles, P, Aneja
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Crystal Structure of Substrate Complexes of Methylmalonyl-CoA Mutase
Biochemistry, 1999X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and 3-carboxypropyl-CoA (substrate and product analogues) show that the enzyme-substrate interactions change little during the course of the rearrangement reaction, in contrast to the large conformational change on ...
F, Mancia, G A, Smith, P R, Evans
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Purification and characterization of methylmalonyl-CoA mutase from Ascaris lumbricoides
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1984Methylmalonyl CoA mutase from Ascaris lumbricoides has been purified to homogeneity. The mutase is homogeneous as judged by equilibrium sedimentation and polyacrylamide gel electrophoresis. The worm mutase is a glycoprotein with a mol. wt of 147,000 +/- 3500 composed of two identical or very similar subunits.
Y S, Han, J M, Bratt, H P, Hogenkamp
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Quantitative measurement of the error in the cryptic stereospecificity of methylmalonyl‐CoA mutase
European Journal of Biochemistry, 1987Samples of methylmalonyl‐CoA and (2H3)methylmalonyl‐CoA were prepared by a combination of chemical and enzymic methods. After ion‐exchange chromatography the unlabelled methylmalonyl‐CoA was pure, the deuterated substance contained 11 – 12% dephospho‐CoA derivative.
M, Michenfelder, W E, Hull, J, Rétey
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Tritium Isotope Effects in Adenosylcobalamin-Dependent Methylmalonyl-CoA Mutase
Biochemistry, 1996Methylmalonyl-CoA mutase from Propionibacterium shermanii is an adenosylcobalamin-dependent enzyme which catalyzes the reversible isomerization of methylmalonyl-CoA and succinyl-CoA. The rate of tritium loss from 5'-[3H]adenosylcobalamin during the enzymic reaction and the relative rates of tritium appearance in substrate and product were examined ...
T W, Meier, N H, Thomä, P F, Leadlay
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Protection and reactivation of human methylmalonyl-CoA mutase by MMAA protein
Biochemical and Biophysical Research Communications, 2011Previous studies have reported that some adenosylcobalamin-dependent enzymes suffer inactivation during catalysis due to the oxidation of cobalamin. In addition, the protection or reactivation of their catalytic activities by proteins called "protectases" or reactivases is well known in bacteria.
Tóshiko, Takahashi-Íñiguez +3 more
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Host expression of methylmalonyl-CoA mutase and tuberculosis: A missing link?
Medical Hypotheses, 2011Bovine tuberculosis (bTB) is a disease caused by Mycobacterium bovis and closely related species of the Mycobacterium tuberculosis complex. bTB is an important health problem affecting livestock, wild animals and accounting for up to 10% of human TB cases worldwide.
Fuente, José de la +3 more
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