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Literature summary for 3.5.4.36 extracted from

  • Xie, K.; Sowden, M.P.; Dance, G.S.; Torelli, A.T.; Smith, H.C.; Wedekind, J.E.
    The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1 (2004), Proc. Natl. Acad. Sci. USA, 101, 8114-8119.
    View publication on PubMedView publication on EuropePMC
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28192
-
 x * 28192, APOBEC-1 from human has proven difficult to purify at levels sufficient for structural studies. Cytosine deaminase from Saccharomyces cerevisiae (CDD1) can be purified readily, which is relevant due to its orthology with APOBEC-1 at the level of both cytidine deaminase (CDA) sequence similarity (27%) and mRNA-editing activity on apolipoprotein B (apoB) substrates. Crystal structure of ScCDD1 is determined to 2.0 A resolution, which reveals that the fundamental CDA fold is necessary and sufficient for C-to-U deamination in pyrimidine metabolism, as well as RNA editing. The data from the CDD1 structure provide the basis for comparative modeling of the APOBEC-1 structure Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P41238
-
-

Subunits

Subunits Comment Organism
? x * 28192, APOBEC-1 from human has proven difficult to purify at levels sufficient for structural studies. Cytosine deaminase from Saccharomyces cerevisiae (CDD1) can be purified readily, which is relevant due to its orthology with APOBEC-1 at the level of both cytidine deaminase (CDA) sequence similarity (27%) and mRNA-editing activity on apolipoprotein B (apoB) substrates. Crystal structure of ScCDD1 is determined to 2.0 A resolution, which reveals that the fundamental CDA fold is necessary and sufficient for C-to-U deamination in pyrimidine metabolism, as well as RNA editing. The data from the CDD1 structure provide the basis for comparative modeling of the APOBEC-1 structure Homo sapiens