Literature summary extracted from

Brown, G.W.; Ray, D.S.
Purification and characterization of DNA ligase I from the trypanosomatid Crithidia fasciculata (1992), Nucleic Acids Res., 20, 3905-3910.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
6.5.1.1	K+	50 mM, 50% inhibition	Crithidia fasciculata
6.5.1.1	NEM	-	Crithidia fasciculata

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
6.5.1.1	0.00034	-	ATP	-	Crithidia fasciculata

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
6.5.1.1	Mg2+	required	Crithidia fasciculata

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
6.5.1.1	80000	-	gel filtration, glycerol density gradient sedimentation	Crithidia fasciculata

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.5.1.1	Crithidia fasciculata	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
6.5.1.1	DNA ligase I	Crithidia fasciculata

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
6.5.1.1	additional information	-	-	Crithidia fasciculata

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6.5.1.1	ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m	joins oligo(rA) annealed to poly(dT) with 250fold lower efficiency than it joins oligo(dT) annealed to poly(dA), ligates blunt-ended DNA fragments in the presence of 15% polyethylene glycol 80000	Crithidia fasciculata	AMP + diphosphate + (deoxyribonucleotide)n+m	-	?

Subunits

EC Number	Subunits	Comment	Organism
6.5.1.1	monomer	x * 80000, SDS-PAGE	Crithidia fasciculata

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
6.5.1.1	50	-	K+	-	Crithidia fasciculata

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Release 2023.1 (January 2023)