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Literature summary for 5.6.2.1 extracted from

  • Das, B.B.; Bose Dasgupta, S.; Ganguly, A.; Mazumder, S.; Roy, A.; Majumder, H.K.
    Leishmania donovani bisubunit topoisomerase I gene fusion leads to an active enzyme with conserved type IB enzyme function (2007), FEBS J., 274, 150-163.
    View publication on PubMed
Search for more literature for 5.6.2.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in Escherichia coli Leishmania donovani

Protein Variants

Protein Variants Comment Organism
H453A Very little relaxing activity detectable, activity of the H453A protein to be more than 100fold reduced compared with that of LdTOPIL-fus-S Leishmania donovani
H453Q Lower activity than LdTOPIL-fus-S, failing to completely relax the supercoiled DNA even after 40 min Leishmania donovani
additional information in vitro gene fusion of Leishmania bisubunit topoisomerase I into a single ORF encoding a new monomeric topoisomerase I (LdTOPIL-fus-S), N-terminal truncation mutant (1–210 amino acids) of the small subunit, when fused to the intact large subunit [LdTOPIL-fus-D(1–210)S], shows reduced topoisomerase I activity and camptothecin sensitivity in comparison to LdTOPIL-fus-S experiments in which Leishmania bisubunit topoisomerase I large subunit (LdTOPIL) and small subunit (LdTOPIS) genes are fused into a single ORF encoding a new topoisomerase I (LdTOPIL-fus-S), suicidal cleavage activity and religation activity of LdTOPIL-fus-S and its mutant variants Leishmania donovani

Inhibitors

Inhibitors Comment Organism Structure
camptothecin Effect of CPT on the relaxation activity and equilibrium cleavage activity of fused topoisomerase I variants Leishmania donovani

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 smaller catalytic subunit with the active site residue Leishmania donovani
73000
-
 full-length larger subunit as the core DNA-binding subunit with the conserved catalytic His at position 453 Leishmania donovani
79000
-
 N-terminal truncated small subunit (amino acids 211–262) fuse to intact large subunit to generate an ORF, LdTOPIL-fus-D(1–210)S Leishmania donovani
102000
-
 Leishmania bisubunit topoisomerase I fusion construct, LdTOPIL and LdTOPIS and the deduced amino acid sequences of the fusion regions Leishmania donovani
102000
-
 point mutations generate at the His453 position of the LdTOPIL-fus-S gene to H453A and H453Q Leishmania donovani
102000
-
 reverse fusion construct of Leishmania bisubunit topoisomerase I, LdTOPIS and LdTOPIL and the deduced amino acid sequences of the fusion regions Leishmania donovani

Organism

Organism UniProt Comment Textmining
Leishmania donovani
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Protein constructs. Structure of recombinant Leishmania donovani topoisomerase I proteins Leishmania donovani

Subunits

Subunits Comment Organism
monomer the kinetoplastid family (Trypanosoma and Leishmania) possess an unusual bisubunit topoisomerase I. In vitro gene fusion of Leishmania bisubunit topoisomerase I into a single ORF encoding a new monomeric topoisomerase I (LdTOPIL-fus-S). This unusual structure of DNA topoisomerase I may provide a missing link in the evolution of type IB enzymes. LdTOPIL-fus-S fusion protein is a functional topoisomerase I. DNA-binding assays shown Leishmania donovani

Synonyms

Synonyms Comment Organism
Topoisomerase I
-
 Leishmania donovani

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 cleavage rates of both LdTOPIL-fus-S and the H453Q mutant LdTOPIL-fus-S proteins at the following pH values: 6.0, 6.5, 7.0, 7.5, 8.0, 8.5, and 9.5 measured. Effect of pH on suicide cleavage rate for LdTOPIL-fus-S and H632Q mutants of LdTOPIL-fus-S proteins Leishmania donovani