Fidelity during cofactor assembly is essential for the proper functioning of metalloenzymes and is ensured by specific chaperones. MeaB, a G-protein chaperone for the coenzyme B12-dependent radical enzyme methylmalonyl-CoA mutase (MCM), uses the energy of GTP binding, hydrolysis or both to regulate cofactor loading into MCM, protect MCM from inactivation and rescue MCM that is inactivated durin...

Fatemeh Sheikhmoonesi*1, MD; Arefeh Shafaat1, MD; Shirin Moarefian2, MD; Talieh Zaman, MD 1. Psychiatry and Behavioral Sciences Research Center, Mazandaran University of Medical Sciences, Sari, Iran 2. Iranian Inherited Metabolic Diseases Association 3. Department of Pediatric, Tehran University of Medical Sciences, Tehran, Iran Received: Jan 20, 2012; Accepted: Jun 27, 2012; First Online Avail...

In mammalian cells, only two enzymes are known to require vitamin B12 (cobalamin, Cbl) derivatives as a cofactor: methionine synthase, a cytosolic enzyme, which uses methylcobalamin, and methylmalonyl-coenzyme A mutase (MCM), a mitochondrial enzyme, which uses 5’-deoxyadenosylcobalamin (AdoCbl) (1). The latter enzyme has a broad distribution among living organisms and is found in both bacteria ...

We describe the use of antisense morpholino oligonucleotides (AMOs) to restore normal splicing caused by intronic molecular defects identified in methylmalonic acidemia (MMA) and propionic acidemia (PA). The three new point mutations described in deep intronic regions increase the splicing scores of pseudoexons or generate consensus binding motifs for splicing factors, such as SRp40, which favo...