-
The epimutation is present in three generations and results from PRDX1 mutations that force antisense transcription of MMACHC.
-
Partial CblC-type inherited Methylmalonic acidemia (MMACHC heterozygous mutation exonl: c. 80A >G, c. 609G >A) can onset with severe metabolic Atypical hemolytic uremic syndrome.
-
The crystal structure of ceCblC provides insights into how architectural differences at the alpha- and beta-faces of cobalamin promote the thiol oxidase activity of ceCblC but mute it in wild-type human CblC.
-
Sequencing of the MMACHC gene is used for confirming the diagnosis of cblC disease. MMACHC mutations were found in all the nine patients. 7 different mutations were identified, including c.609G>A, c.455_457delCCC, c.394C>T, c.445_446insA, c.658_660delAAG, c.452A>G and IVS1+1G>A. The most frequent mutation was c.609G>A (6/9). Two patients had homozygous mutations (c.445_446insA/c.445_446insA and c.609G>A/c.609G>A).
-
Case Report: c.567dupT,p.(Ile190Tyrfs*13) MMACHC heterozygous mutation underlying methylmalonic academia in infant.
-
Five different known mutations in either MUT or MMACHC genes were identified in seven of the eight Chinese patients with methyl malonic acidemia.
-
MMACHC mutation was found in children diagnosed with hemolytic uremic syndrome secondary to cobalamin C disorder.
-
the MMACHC-MMADHC complex is a 1:1 heterodimer, where the interaction region overlaps with the MMACHC-Cbl binding site
-
These results indicated that hypergonadotropic hypogonadism may be a novel clinical manifestation of cblC disease, but more reports on additional patients are needed to support this hypothesis.
-
an adult patient with bull's eye macular lesions and no clinically relevant systemic symptoms was diagnosed with cblC by genetic screening and follow-up biochemical laboratory tests.
-
A novel mutation p.G155R of the MMACHC gene is identified in prenatal diagnosis of combined methylmalonic aciduria and homocystinuria.
-
Results propose a model whereby membrane-bound LMBD1 and ABCD4 facilitate the vectorial delivery of lysosomal vitamin B12 to cytoplasmic MMACHC.
-
mutation analysis of the MMACHC gene in four patients revealed novel heterozygous mutations at nucleotide 276 (c.276G > A [p.Glu926Glu] and c.276G > T [p.Glu92Asp]), which is located at the end of exon 2.
-
HCFC1 plays a role in craniofacial development, which is in part mediated through the regulation of MMACHC expression
-
The gene responsible for cblC, named MMACHC, catalyzes the reductive decyanation of cyanocobalamin.
-
data suggest that the interaction of methionine synthase with MMACHC may play a role in the regulation of the cellular processing of cobalamins that is required for cobalamin cofactor synthesis
-
Subcellular location of MMACHC and MMADHC, two human proteins central to intracellular vitamin B(12) metabolism.
-
The function of MMADHC is exerted through its structured C-terminal domain via interactions with MMACHC.
-
a structural framework provides a framework for understanding catalytic function and disease mechanism for the multifunctional MMACHC complex.
-
MMADHC was confirmed as a binding partner for MMACHC both in vitro (SPR) and in vivo (bacterial two-hybrid system).
