Anti-Methylmalonyl Coenzyme A mutase Antibody Picoband® (monoclonal, 2D6) Fluoro488 Conjugated

Methylmalonyl-CoA mutase (MUT) is a mitochondrial enzyme that catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. This gene is mapped to 6p12.3. MUT requires a vitamin B12-derived prosthetic group, adenosylcobalamin (commonly referred to as AdoCbl), to function. And the product of this enzyme, succinyl-CoA, is a key molecule of the TCA cycle.

Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.

1. Adjalla, C. E., Hosack, A. R., Gilfix, B. M., Lamothe, E., Sun, S., Chan, A., Evans, S., Matiaszuk, N. V., Rosenblatt, D. S. Seven novel mutations in mut methylmalonic aciduria. Hum. Mutat. 11: 270-274, 1998. 2. Berger, I., Shaag, A., Anikster, Y., Baumgartner, E. R., Bar-Meir, M., Joseph, A., Elpeleg, O. N. Mutation analysis of the MCM gene in Israeli patients with mut (0) disease. Molec. Genet. Metab. 73: 107-110, 2001. 3. Cavicchi, C., Donati, M. A., Funghini, S., la Marca, G., Malvagia, S., Ciani, F., Poggi, G. M., Pasquini, E., Zammarchi, E., Morrone, A. Genetic and biochemical approach to early prenatal diagnosis in a family with mut methylmalonic aciduria. Clin. Genet. 69: 72-76, 2006.