EC Number   |
General Information |
Reference |
|---|
   1.14.18.2 | evolution |
CMAH phylogenetic analysis, genotyping and genotype-phenotype correlation analysis of gene CMAH and blood typa A, B, or AB in cat breeds, overview |
746206 |
| 1.14.18.2 | evolution |
detailed phylogenetic analysis, overview |
745641 |
| 1.14.18.2 | evolution |
gene CMAH, genotyping, genetic structure, and phylogenetic analysis. Haplotype inference, which is focused on non-synonymous single-nucleotide polymorphisms reveals that eight haplotypes carry one to four mutations in CMAH, and all cats with type B (n = 34) and AB (n = 2) blood carry two alleles derived from the mutated CMAH gene |
746215 |
| 1.14.18.2 | malfunction |
by inactivating enzyme CMAH, the NeuAc precursor accumulates and NeuGc is absent on the erythrocyte cell surface, thus reducing parasite infection in humans and promoting a positive selection during evolution, which results in the enrichment of resistant blood type antigens |
746206 |
| 1.14.18.2 | malfunction |
mice bearing a human-like deletion of the Cmah gene exhibit fasting hyperglycemia and glucose intolerance following a high-fat diet. This phenotype is caused by compromised pancreatic beta-cell function associated with a 65% decrease in islet size and area and 50% decrease in islet number. Obese Cmah-null mice also show an 40% reduction in response to insulin secretagogues in vivo |
711964 |
| 1.14.18.2 | malfunction |
pcmah silencing by short hairpin RNA results in a decrease in N-glycolylneuraminic acid content and xenoantigenicity in pig kidney PK15 cells |
711142 |
| 1.14.18.2 | malfunction |
sera obtained from CMAH-/- mice and healthy human volunteers having anti- N-glycolylneuraminic acid Abs initiate complement-mediated lysis against CMAH+/+ cells in vitro. Cytotoxic activity of anti- N-glycolylneuraminic acid Abs is also determined in vivo: N-glycolylneuraminic acid CMAH+/+ mouse splenocytes that had been i.v. injected are completely eliminated in syngeneic CMAH-/- mice |
712638 |
| 1.14.18.2 | more |
sequence-based, three-dimensional enzyme structure modeling, overview |
744458 |
| 1.14.18.2 | physiological function |
cytidine monophospho-N-acetylneuraminic acid hydroxylase (CMAH) is associated with the production of the sialic acids present on cat erythrocytes. CMAH converts N-acetylneuraminic acid (NeuAc) to N-glycolylneuraminic acid (NeuGc) by substituting one of the hydrogen atoms in the methyl moiety with a carboxyl group. A genetic variant of enzyme CMAH is associated with blood type AB in Ragdoll cats |
746206 |
| 1.14.18.2 | physiological function |
enzyme CMP-N-acetylneuraminic acid hydroxylase (CMAH) is responsible for the synthesis of N-glycolylneuraminic acid (Neu5Gc), a sialic acid present on the cell surface proteins of most deuterostomes. CMAH is the only enzyme capable of synthetizing Neu5Gc |
745641 |
