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Literature summary for 3.5.4.38 extracted from

  • Pham, P.; Afif, S.A.; Shimoda, M.; Maeda, K.; Sakaguchi, N.; Pedersen, L.C.; Goodman, M.F.
    Structural analysis of the activation-induced deoxycytidine deaminase required in immunoglobulin diversification (2016), DNA Repair, 43, 48-56 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion technique at 4°C, crystal structure of enzyme variant AIDv(DELTA15), at 2.8 A resolution Escherichia coli O157:H7

Protein Variants

Protein Variants Comment Organism
K52A 2fold reduction in processivity Escherichia coli O157:H7
Q175A 2fold reduction in processivity Escherichia coli O157:H7
R171A 2fold reduction in processivity Escherichia coli O157:H7
R178A 2fold reduction in processivity Escherichia coli O157:H7

Organism

Organism UniProt Comment Textmining
Escherichia coli O157:H7 P0AEY0
-
-

Purification (Commentary)

Purification (Comment) Organism
Sf9 expressed GST-tagged enzyme Escherichia coli O157:H7

Synonyms

Synonyms Comment Organism
AID
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Escherichia coli O157:H7

General Information

General Information Comment Organism
physiological function the enzyme initiates somatic hypermutation and class-switch recombination by deaminating C -> U during transcription of Ig-variable and Ig-switch region DNA, which is essential to produce high-affinity antibodies Escherichia coli O157:H7