Purification and properties of methylmalonyl coenzyme A mutase from human liver☆
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2022, Journal of Food Composition and AnalysisDetermination of cobalamin and related compounds in foods
2022, Vitamins and HormonesMUT gene variants in patients with methylmalonic acidemia in Bangladeshi population and their distinguishing metabolic profiles
2021, Meta GeneCitation Excerpt :It encodes a 750 amino acid precursor protein, which is transported into the mitochondrial matrix and processed by the removal of 32 amino acid long mitochondrial leader sequence (Jansen et al., 1989; Ledley et al., 1988a). The functional MCM enzyme is formed through homodimerization of the 718 amino acid long subunits with 1 molecule of adenosylcobalamin bound to each of the subunits (Fenton et al., 1982). 258 pathogenic mutations in MUT have been detected in different populations (Stenson et al., 2012).
Human MMAA induces the release of inactive cofactor and restores methylmalonyl-CoA mutase activity through their complex formation
2017, BiochimieCitation Excerpt :Such a result has probably not been reported before because high substrate concentrations were used in preceding works, thus precluding this observation. To determine if hMMAA modifies the kinetic parameters of hMCM for the cofactor, an attempt to purify and reconstitute the apo-hMCM protein with different concentrations of AdoCbl was performed and unsuccessful, due to the previously reported instability of the human apoenzyme [25]. From the immunofluorescence assays in human fibroblasts, we could observe that the two human proteins are distributed in both the cytoplasm and mitochondria and that hMCM is in greater abundance than hMMAA.
Nutrition and Atherosclerosis
2015, Archives of Medical Research
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This work was supported by Grant AM 09527 from the National Institutes of Health.
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Present address: Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Md. 21205.
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H.F.W. was the recipient of a traineeship from the National Institutes of Health (T01-GM 02299).
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Present address: Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University, Rehovot, Israel.