Results 41 to 50 of about 80,661 (193)

Metabolic phenotype of methylmalonic acidemia in mice and humans: the role of skeletal muscle

BMC Medical Genetics, 2007
Background Mutations in methylmalonyl-CoA mutase cause methylmalonic acidemia, a common organic aciduria. Current treatment regimens rely on dietary management and, in severely affected patients, liver or combined liver-kidney transplantation.
Kaestner Klaus H, Allen Robert, Stabler Sally, Tsai Matthew, Fu Hong, Sloan Jennifer, Chandler Randy J, Kazazian Haig H, Venditti Charles P   +8 more
doaj   +1 more source

Different mutations in the MMUT gene are associated with the effect of vitamin B12 in a cohort of 266 Chinese patients with mut‐type methylmalonic acidemia: A retrospective study

Molecular Genetics & Genomic Medicine, 2021
Background To summarize the relationship between different MMUT gene mutations and the response to vitamin B12 in MMA. Methods This was a retrospective study of patients diagnosed with mut‐type MMA.
Yue Yu, Ruixue Shuai, Lili Liang, Wenjuan Qiu, Linghua Shen, Shengnan Wu, Haiyan Wei, Yongxing Chen, Chiju Yang, Peng Xu, Xigui Chen, Hui Zou, Jizhen Feng, Tingting Niu, Haili Hu, Jun Ye, Huiwen Zhang, Deyun Lu, Zhuwen Gong, Xia Zhan, Wenjun Ji, Xuefan Gu, Lianshu Han   +22 more
doaj   +1 more source

Decrease of disease‐related metabolites upon fasting in a hemizygous knock‐in mouse model (Mut‐ko/ki) of methylmalonic aciduria

JIMD Reports, 2021
Methylmalonyl‐CoA mutase (MMUT) is part of the propionyl‐CoA catabolic pathway, responsible for the breakdown of branched‐chain amino acids, odd‐chain fatty acids and the side‐chain of cholesterol.
Marie Lucienne, Déborah Mathis, Nathan Perkins, Ralph Fingerhut, Matthias R. Baumgartner, D. Sean Froese   +5 more
doaj   +1 more source

Structure of the human methylmalonyl-CoA mutase (MUT) locus

Genomics, 1990
The MUT locus encoding the enzyme methylmalonyl-CoA mutase is defective in mut forms of methylmalonic acidemia. This locus has been mapped to chromosome 6p12-21.1. We report cloning and characterization of this locus which comprises 13 exons spanning greater than 35 kb of the genome.
S U, Nham, M F, Wilkemeyer, F D, Ledley
openaire   +2 more sources

Transcriptomic and proteomic changes associated with cobalamin-dependent propionate production by the rumen bacterium Xylanibacter ruminicola

mSystems
Xylanibacter ruminicola is an abundant rumen bacterium that produces propionate in a cobalamin (vitamin B12)-dependent manner via the succinate pathway.
Sam C. Mahoney-Kurpe, Nikola Palevich, Dragana Gagic, Patrick J. Biggs, Peter M. Reid, Ianina Altshuler, Phillip B. Pope, Graeme T. Attwood, Christina D. Moon   +8 more
doaj   +1 more source

The masked cysteine residues in methylmalonyl-CoA mutase from Propionibacterium shermanii are essential for catalytic activity

, 1996
Two masked cysteine residues have been reported in methylmalonyl-CoA mutase from Propionibacterium shermanii, Cys-535 in the α-subunit and Cys-517 in the β-unit, which are revealed only after reduction of the denatured enzyme with dithiothreitol.
Roy, I.
core   +1 more source

Pre-implantation genetic diagnosis in an Iranian family with a novel mutation in MUT gene

BMC Medical Genetics, 2020
Background Methylmalonic acidemia (MMA), which is an autosomal recessive metabolic disorder, is caused by mutations in methylmalonyl-CoA mutase (MUT) gene.
Parham Habibzadeh, Zahra Tabatabaei, Mohammad Ali Farazi Fard, Laila Jamali, Aazam Hafizi, Pooneh Nikuei, Leila Salarian, Mohammad Hossein Nasr Esfahani, Zahra Anvar, Mohammad Ali Faghihi   +9 more
doaj   +1 more source

Novel AAV-mediated genome editing therapy improves health and survival in a mouse model of methylmalonic acidemia.

PLoS ONE, 2022
Methylmalonic acidemia (MMA) is an inborn error of metabolism mostly caused by mutations in the mitochondrial methylmalonyl-CoA mutase gene (MMUT). MMA patients suffer from frequent episodes of metabolic decompensation, which can be life threatening.
Shengwen Zhang, Amy Bastille, Susana Gordo, Nikhil Ramesh, Jenisha Vora, Elizabeth McCarthy, Xiaohan Zhang, Dylan Frank, Chih-Wei Ko, Carmen Wu, Noel Walsh, Shreya Amarwani, Jing Liao, Qiang Xiong, Lauren Drouin, Matthias Hebben, Kyle Chiang, B Nelson Chau   +17 more
doaj   +2 more sources

A protein having similarity with methylmalonyl-CoA mutase is required for the assimilation of methanol and ethanol by Methylobacterium extorquens AM1 [PDF]

, 1996
A 4.0 kb region of Methylobacterium extorquens AM1 DNA which complements three mutants unable to convert acetyl-CoA to glyoxylate (and therefore defective in the assimilation of methanol and ethanol) has been isolated and sequenced.
Smith, Loraine M., Dijkhuizen, Lubbert; id_orcid, Meijer, Wim G., Goodwin, Pat M., Dijkhuizen, Lubbert, W. G. Meijer, L. Dijkhuizen, L. M. Smith, P. M. Goodwin   +8 more
core   +1 more source

Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new subclade of coenzyme B12-dependent acyl-CoA mutases

, 2008
Coenzyme B(12)-dependent mutases are radical enzymes that catalyze reversible carbon skeleton rearrangement reactions. Here we describe Rhodobacter sphaeroides ethylmalonyl-CoA mutase (Ecm), a novel member of the family of coenzyme B(12)-dependent acyl ...
Retey, J., Alber, B., Fuchs, G., Erb, T.
core   +1 more source