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MMAB encodes a protein that catalyzes the final step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12-containing coenzyme for methylmalonyl-CoA mutase. Additionally we are shipping Methylmalonic Aciduria (Cobalamin Deficiency) CblB Type Antibodies (37) and Methylmalonic Aciduria (Cobalamin Deficiency) CblB Type Kits (4) and many more products for this protein.
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analysis of how molecular chaperones interact with ATR in methylmalonic aciduria cblB type
MMAB might be a target and potential biomarker of hepatotoxicity in EFV-induced liver toxicity
These findings suggest that rs11066782 in KCTD10, rs11613718 in KCTD10 and rs11067233 in MMAB may contribute to the susceptibility of coronary heart disease by altering plasma HDL-C levels in Han Chinese.
MMAB mutations, including one novel nonsense mutation (c.12 C>A [p.C4X]), were identified in all members of the cblB cohort.
Pathogenicity of the human truncation mutant results from its inability to sequester AdoCbl for direct transfer to methylmalonyl-CoA mutase, resulting in holoenzyme formation.
c.584G>A, c.349-1G>C, and c.290G>A mutations affect the splicing process of ATR.
These data suggest MMAB is the most likely gene influencing high-density lipoprotein-cholesterol levels at MMAB-MVK locus.
Characterization of ligand-binding by MMAB provides insight into the mechanism of cobalamin adenosylation and the effect of patient mutations in the inherited disorder
report the identification of ATR cDNA as well as the corresponding gene; ATR expression is altered in cell lines derived from cblB methylmalonyl aciduria patients; propose that inborn errors in the ATR gene identified here result in methylmalonyl aciduria
Results describe two common polymorphic variants of ATP:cob(I)alamin adenosyltransferase that are found in normal individuals, and their interactions with methionine synthase reductase.
Mutations in methylmalonic aciduria type B protein is associated with methylmalonic acidemia
Long-term outcome in methylmalonic acidurias is influenced by the underlying genetic defects in MCM/MMAA/MMAB.
Methylmalonic acidaemia: examination of genotype and biochemical data in 32 patients belonging to mut, cblA or cblB complementation group.
Results functionally defined the hATR active site and tentatively implicated three amino acid residues in facilitating the reduction of cob(II)alamin to cob(I)alamin which is a prerequisite to adenosylation.
homozygotes for the major allele (G) at MMAB_3U3527G-->C had higher LDL-cholesterol concentrations than did carriers of the minor allele (P = 0.034).
report the isolation of an ATR cDNA, from a bovine liver library, by complementation of an ATR-deficient Salmonella mutant.
The mouse methylmalonic aciduria- related genes, Mmaa, Mmab, and Mut may have specialized functions depending on the tissue or cell type.
This gene encodes a protein that catalyzes the final step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12-containing coenzyme for methylmalonyl-CoA mutase. Mutations in the gene are the cause of vitamin B12-dependent methylmalonic aciduria linked to the cblB complementation group. Alternatively spliced transcript variants have been found.
, ATP:corrinoid adenosyltransferase
, aquocob(I)alamin vitamin B12s adenosyltransferase
, cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
, methylmalonic aciduria type B protein
, cob(I)alamin adenosyltransferase
, methylmalonic aciduria (cobalamin deficiency) type B
, methylmalonic aciduria type B homolog
, ATP:Cob(I)alamin Adenosyltransferase