Literature summary for 6.5.1.1 extracted from

Pitcher, R.S.; Tonkin, L.M.; Green, A.J.; Doherty, A.J.
Domain structure of a NHEJ DNA repair ligase from Mycobacterium tuberculosis (2005), J. Mol. Biol., 351, 531-544.

Search for more literature for 6.5.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
separate polymerase, nuclease and ligase domains of Mt-Lig are cloned individually, over-expressed in Escherichia coli B834	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
separate polymerase, nuclease and ligase domains of Mt-Lig cloned individually and over-expressed in Escherichia coli B834	Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m	the polymerase domain has DNA-dependent RNA primase activity, catalysing the synthesis of unprimed oligoribonucleotides on single-stranded DNA templates. The polymerase domain can also extend DNA in a template-dependent manner. The ligase domain catalyses the sealing of nicked double-stranded DNA designed to mimic a double-strand break, consistent with the role of Mt-Lig in non-homologous end-joining. The nuclease domain did not function independently as a 3'-5' exonuclease. Both the polymerase and ligase domains bind DNA in vitro, the latter with considerably higher affinity	Mycobacterium tuberculosis	AMP + diphosphate + (deoxyribonucleotide)m+n	-	?

Synonyms

Synonyms	Comment	Organism
Mt-Lig	-	Mycobacterium tuberculosis
NHEJ DNA repair ligase	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)