ExplorEnz: EC 3.5.4.38

Your query returned 1 entry. Printable version

3.5.4.38

Accepted name:

single-stranded DNA cytosine deaminase

Reaction:

cytosine in single-stranded DNA + H₂O = uracil in single-stranded DNA + NH₃

Other name(s):

AID; activation-induced deaminase; AICDA (gene name); activation-induced cytidine deaminase

Systematic name:

single-stranded DNA cytosine aminohydrolase

Comments:

The enzyme exclusively catalyses deamination of cytosine in single-stranded DNA. It preferentially deaminates five-nucleotide bubbles. The optimal target consists of a single-stranded NWRCN motif (W = A or T, R = A or G) [2]. The enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Sohail, A., Klapacz, J., Samaranayake, M., Ullah, A. and Bhagwat, A.S. Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations. Nucleic Acids Res. 31 (2003) 2990–2994. [PMID: 12799424]
2.	Larijani, M., Petrov, A.P., Kolenchenko, O., Berru, M., Krylov, S.N. and Martin, A. AID associates with single-stranded DNA with high affinity and a long complex half-life in a sequence-independent manner. Mol. Cell Biol. 27 (2007) 20–30. [DOI] [PMID: 17060445]
3.	Brar, S.S., Sacho, E.J., Tessmer, I., Croteau, D.L., Erie, D.A. and Diaz, M. Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA. DNA Repair (Amst.) 7 (2008) 77–87. [DOI] [PMID: 17889624]
4.	Larijani, M. and Martin, A. Single-stranded DNA structure and positional context of the target cytidine determine the enzymatic efficiency of AID. Mol. Cell Biol. 27 (2007) 8038–8048. [DOI] [PMID: 17893327]
5.	Verma, S., Goldammer, T. and Aitken, R. Cloning and expression of activation induced cytidine deaminase from Bos taurus. Vet. Immunol. Immunopathol. 134 (2010) 151–159. [DOI] [PMID: 19766322]

[EC 3.5.4.38 created 2013]