Literature summary for 6.5.1.1 extracted from

Kito, H.; Fujikawa, T.; Moriwaki, A.; Tomono, A.; Izawa, M.; Kamakura, T.; Ohashi, M.; Sato, H.; Abe, K.; Nishimura, M.
MgLig4, a homolog of Neurospora crassa Mus-53 (DNA ligase IV), is involved in, but not essential for, non-homologous end-joining events in Magnaporthe grisea (2008), Fungal Genet. Biol., 45, 1543-1551.

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Protein Variants

Protein Variants	Comment	Organism
additional information	mutants (mglig4) show no defects in asexual or sexual growth, and are fully pathogenic, compared to the wild type enzyme, mglig4 exhibits weak sensitivity to a DNA-damaging agent camptothecin, non-homologous integration of DNA is frequently observed in mglig4 transformants	Pyricularia grisea

Inhibitors

Inhibitors	Comment	Organism	Structure
camptothecin	-	Pyricularia grisea

Organism

Organism	UniProt	Comment	Textmining
Pyricularia grisea	B6ZH51	strains Guy11 and P2	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m	-	Pyricularia grisea	AMP + diphosphate + (deoxyribonucleotide)m+n	-	?

Synonyms

Synonyms	Comment	Organism
DNA ligase	-	Pyricularia grisea
Lig4	Lig4 is involved in, but not essential for, the non-homologous end-joining system in Magnaporthe grisea	Pyricularia grisea

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Pyricularia grisea

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Release 2023.1 (January 2023)