An ATP-independent catenating enzyme from the kinetoplast hemoflagellate Leishmania donovani.
An enzyme from Leishmania donovani that catenates monomeric pBR322 into huge catenanes has been isolated and characterized. The enzyme also decatenates kinetoplast DNA networks into covalently closed monomeric circles and relaxes supercoiled pBR322. The catenation, decatenation and relaxation reactions do not require ATP. The formation of topological isomers of unique linking numbers suggest that the enzyme is a type II DNA topoisomerase.
Chakraborty
A K
AK
Molecular Parasitology Laboratory, Indian Institute of Chemical Biology, Calcutta.
Majumder
H K
HK
D000255:Adenosine Triphosphate; D000818:Animals; D002852:Chromatography, Ion Exchange; D004250:DNA Topoisomerases, Type II / Q000032:analysis / Q000302:isolation & purification*; D004278:DNA, Superhelical / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D007893:Leishmania donovani / Q000201:enzymology*
D004278:DNA, Superhelical; D000255:Adenosine Triphosphate; D004250:DNA Topoisomerases, Type II