terminal deoxynucleotidyltransferase (terminal addition enzyme, terminal deoxynucleotidyltransferase, terminal transferase, DNTT, TDT)
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Function
- template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator
- one of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain & T-cell receptor gene segments during maturation of B-cells & T-cells
- interacts with PRP19 & DNTTIP1
- forms a ternary complex with DNTTIP2 & core histone, released from DNTTIP2/core histone complex by PCNA
deoxynucleoside triphosphate + DNA(n) <--> diphosphate + DNA(n+1)
Cofactor: Mg+2
Structure
- belongs to the DNA polymerase type-X family
- contains 1 BRCT domain
Compartment
Pathology
- very high levels of enzyme activity have been detected in certain acute leukemic cells
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P04053.html
- ↑ Tietz Fundamentals of Clinical Chemistry 3rd ed, WB Saunders, 1987 pg 413