Results 161 to 170 of about 76,676 (194)
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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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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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[35] 2-methylmalonyl-CoA mutase from Propionibacterium shermanii (methylmalonyl-CoA isomerase)
1969Publisher Summary This chapter discusses the 2-Methylmalonyl-CoA Mutase from Propionibacterium shermanii in depth. The bacteria are grown, harvested, and extracted. Methylmalonyl-CoA-2- 14 C is converted by enzymatic isomerization to succinyl-CoA-3- 14 C.
R.W. Kellermeyer, Harland G. Wood
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Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase
Human Genetics, 1992We have previously identified a mutation in the gene for methylmalonyl CoA mutase in a patient with the mut- phenotype of methylmalonic aciduria. This mutation (G717V) interferes with the binding of the deoxyadenosylcobalamin cofactor to the apoenzyme producing a mutant holoenzyme that is defective, but not completely inactive, in vitro.
A M, Crane +3 more
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Archives of Microbiology, 2003
High activity (>60 munit/mg protein) of 5'-deoxyadenosylcobalamin-dependent methylmalonyl-CoA mutase (EC 5.4.99.2) was constantly found during growth of a strain of the root-nodule-forming bacterium Sinorhizobium meliloti harboring an extra plasmid-encoded copy of the methylmalonyl-CoA-mutase-encoding bhbA gene.
Emi, Miyamoto +5 more
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High activity (>60 munit/mg protein) of 5'-deoxyadenosylcobalamin-dependent methylmalonyl-CoA mutase (EC 5.4.99.2) was constantly found during growth of a strain of the root-nodule-forming bacterium Sinorhizobium meliloti harboring an extra plasmid-encoded copy of the methylmalonyl-CoA-mutase-encoding bhbA gene.
Emi, Miyamoto +5 more
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Assembly and Protection of the Radical Enzyme, Methylmalonyl-CoA Mutase, by Its Chaperone
Biochemistry, 2006MeaB is a recently described P-loop GTPase that plays an auxiliary role in the reaction catalyzed by the radical B12 enzyme, methylmalonyl-CoA mutase. Defects in the human homologue of MeaB result in methylmalonic aciduria, but the role of this protein in coenzyme B12 assimilation and/or utilization is not known.
Dominique, Padovani, Ruma, Banerjee
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[34] Methylmalonyl-CoA mutase from sheep liver
1969Publisher Summary The chapter describes the method used routinely for purification of the enzyme from sheep liver. Several methods are available for the assay of methylmalonyl-CoA mutase. All operations are carried out at 0-4° unless otherwise stated. The protein values given in connection with the purification procedure are spectrophotometric values.
Rajarshi Mazumder, Severo Ochoa
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Mechanistic and structural studies on methylmalonyl-CoA mutase
Biochemical Society Transactions, 1998N H, Thomä, P F, Leadlay
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Biochemical and Biophysical Research Communications, 1964
M. Sprecher, M.J. Clark, D.B. Sprinson
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M. Sprecher, M.J. Clark, D.B. Sprinson
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