Apolipoprotein B mRNA editing catalytic polypeptide 1 (APOBEC1)

Apolipoprotein B mRNA editing catalytic polypeptide 1 (APOBEC1) is a zinc-dependent cytidine deaminase that serves as the catalytic core of the ApoB mRNA editing complex (PubMed: 8033212). Its primary physiological role is the site-specific deamination of cytosine to uracil at position 6666 of the apolipoprotein B (ApoB) mRNA in the small intestine, which creates a premature stop codon and results in the production of the truncated ApoB-48 isoform necessary for lipid absorption (UniProt P41238). Beyond its role in lipid metabolism, APOBEC1 has become a cornerstone of modern biotechnology as the effector domain in cytosine base editors (CBEs), enabling precise C-to-T transitions in the genome for therapeutic purposes (Nature: 27196570). However, its ability to act on single-stranded DNA also makes it a potential source of genomic instability; aberrant expression is associated with high mutational burdens and the progression of various cancers (PubMed: 25512524). Consequently, APOBEC1 is viewed both as a powerful tool for gene correction and a target for monitoring or inhibition in the context of oncogenic mutagenesis.

Other names

APOBEC-1Apolipoprotein B mRNA editing enzyme 1HEIBEDPC-to-U editing enzyme APOBEC1

Catalyzes the hydrolytic deamination of cytidine to uridine in mRNA or deoxycytidine to deoxyuridine in single-stranded DNA (UniProt P41238).