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Studies on Methylmalonyl-CoA Mutase from Escherichia coli [PDF]
, 2008 Methylmalonyl-CoA mutase (MCM, E.C. 5.4.99.2), a coenzyme B12-dependent enzyme, catalyses the inter conversion of succinyl-CoA and methylmalonyl-CoA. The gene (sbm) encoding this enzyme is found in Escherichia coli (E. coli) at 62.3min on the E. coli chromosome. However, the metabolic role of this enzyme in the organism is not known.
Kannan, S.M.
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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.
Maria Elena Flores +2 more
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Intragenic complementation in methylmalonyl CoA mutase
, 1994 Methylmalonic aciduria (MMA) is an autosomal recessive metabolic disorder with an incidence of 1 in 48,000, which may be due to a defect in the mitochondrial homodimeric enzyme methylmalonyl CoA mutase (mut MMA). mut MMA is subdivided into $mut sp circ$ and $mut sp-$ subclasses on the basis of complementation analysis; $mut sp circ$ cell lines have ...
Farah, Rita S.
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A radio-HPLC assay for the measurement of methylmalonyl-CoA mutase
Clinica Chimica Acta, 1984Kim Bartlett, K Bartlett
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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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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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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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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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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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