Tyrosyl-DNA phosphodiesterase 1 is an
enzyme that in humans is encoded by the TDP1gene.[5][6][7]
The
protein encoded by this gene is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the
hydrolysis of the
phosphodiester bond between the
tyrosine residue of
Type I topoisomerase and the 3-prime
phosphate of
DNA. This protein may also remove
glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of
free-radical mediated DNA double-strand breaks.
This gene is a member of the
phospholipase D family and contains two PLD phosphodiesterase domains.
Mutations in this gene are associated with the disease
spinocerebellar ataxia with axonal neuropathy (SCAN1). While several
transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same
isoform.[7]
Davies DR, Interthal H, Champoux JJ, Hol WG (2003). "Insights into substrate binding and catalytic mechanism of human tyrosyl-DNA phosphodiesterase (Tdp1) from vanadate and tungstate-inhibited structures". J. Mol. Biol. 324 (5): 917–32.
doi:
10.1016/S0022-2836(02)01154-3.
PMID12470949.
Davies DR, Interthal H, Champoux JJ, Hol WG (2004). "Explorations of peptide and oligonucleotide binding sites of tyrosyl-DNA phosphodiesterase using vanadate complexes". J. Med. Chem. 47 (4): 829–37.
doi:
10.1021/jm030487x.
PMID14761185.
Raymond AC, Rideout MC, Staker B, et al. (2004). "Analysis of human tyrosyl-DNA phosphodiesterase I catalytic residues". J. Mol. Biol. 338 (5): 895–906.
doi:
10.1016/j.jmb.2004.03.013.
PMID15111055.
Yang M, Kirley TL (2004). "Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change". Biochemistry. 43 (28): 9185–94.
doi:
10.1021/bi049565o.
PMID15248776.
Tyrosyl-DNA phosphodiesterase 1 is an
enzyme that in humans is encoded by the TDP1gene.[5][6][7]
The
protein encoded by this gene is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the
hydrolysis of the
phosphodiester bond between the
tyrosine residue of
Type I topoisomerase and the 3-prime
phosphate of
DNA. This protein may also remove
glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of
free-radical mediated DNA double-strand breaks.
This gene is a member of the
phospholipase D family and contains two PLD phosphodiesterase domains.
Mutations in this gene are associated with the disease
spinocerebellar ataxia with axonal neuropathy (SCAN1). While several
transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same
isoform.[7]
Davies DR, Interthal H, Champoux JJ, Hol WG (2003). "Insights into substrate binding and catalytic mechanism of human tyrosyl-DNA phosphodiesterase (Tdp1) from vanadate and tungstate-inhibited structures". J. Mol. Biol. 324 (5): 917–32.
doi:
10.1016/S0022-2836(02)01154-3.
PMID12470949.
Davies DR, Interthal H, Champoux JJ, Hol WG (2004). "Explorations of peptide and oligonucleotide binding sites of tyrosyl-DNA phosphodiesterase using vanadate complexes". J. Med. Chem. 47 (4): 829–37.
doi:
10.1021/jm030487x.
PMID14761185.
Raymond AC, Rideout MC, Staker B, et al. (2004). "Analysis of human tyrosyl-DNA phosphodiesterase I catalytic residues". J. Mol. Biol. 338 (5): 895–906.
doi:
10.1016/j.jmb.2004.03.013.
PMID15111055.
Yang M, Kirley TL (2004). "Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change". Biochemistry. 43 (28): 9185–94.
doi:
10.1021/bi049565o.
PMID15248776.