1.14.18.2: CMP-N-acetylneuraminate monooxygenase
This is an abbreviated version!
For detailed information about CMP-N-acetylneuraminate monooxygenase, go to the full flat file.
Reaction
+ 2 ferrocytochrome b5 + + 2 H+ = + 2 ferricytochrome b5 +
Synonyms
CMAH, CMP Neu5Ac hydroxylase, CMP-N-acetylneuraminate hydroxylase, CMP-N-acetylneuraminate,NAD(P)H:oxygen oxidoreductase (hydroxylating), CMP-N-acetylneuraminic acid hydroxylase, CMP-Neu5Ac hydroxylase, CMP-NeuAc hydroxylase, cytidine monophosphate-N-acetylneuraminic acid hydroxylase, cytidine monophospho-N-acetylneuraminic acid hydroxylase, EC 1.14.13.45, oxygenase, cytidine monophosphoacetylneuraminate mono-, pcmah
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General Information
General Information on EC 1.14.18.2 - CMP-N-acetylneuraminate monooxygenase
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evolution
malfunction
physiological function
additional information
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sequence-based, three-dimensional enzyme structure modeling, overview
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CMAH phylogenetic analysis, genotyping and genotype-phenotype correlation analysis of gene CMAH and blood typa A, B, or AB in cat breeds, overview
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
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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
malfunction
pcmah silencing by short hairpin RNA results in a decrease in N-glycolylneuraminic acid content and xenoantigenicity in pig kidney PK15 cells
malfunction
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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
malfunction
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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
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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
physiological function
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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
physiological function
the cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMAH) gene is associated with the feline AB blood group system, type A and type B antigens are Neu5Gc and Neu5Ac, respectively. Distribution of AB blood group antigens, CMAH gene structure, mutation, diplotypes, and haplotypes of the cat CMAH genes, overview. The feline AB blood group system consists of A and B antigens and contains blood group type A (type A), blood group type B (type B), and the rare blood group type AB (type AB). Type A erythrocytes express N-glycolylneuraminic acid (Neu5Gc) and type B erythrocytes express N-acetylneuraminic acid (Neu5Ac). The enzyme cytidinemonophosphate-N-acetylneuraminic acid hydroxylase synthesizes Neu5Ac to Neu5Gc. type AB erythrocytes have less Neu5Ac than type A erythrocytes and less Neu5Gc than type B erythrocytes
physiological function
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the enzyme is essential for N-glycolylneuraminic acid (Neu5Gc) synthesis