Literature summary for 6.5.1.1 extracted from

Rossi, R.; Montecucco, A.; Ciarrocchi, G.; Biamonti, G.
Functional characterization of the T4 DNA ligase: a new insight into the mechanism of action (1997), Nucleic Acids Res., 25, 2106-2113.

Search for more literature for 6.5.1.1

Protein Variants

Protein Variants	Comment	Organism
K159L	the inactive His-K159L substitution mutant is unable to self-associate, but still possesses AMP-dependent DNA nicking activity, no blunt end ligation. Mutant enzyme His-N-DELTA80 catalyzes no blunt end ligation and no AMP-dependent activity. Mutant enzyme His-C-DELTA57has no blunt end ligation activity, no AMP-dependent activity, low nick joining activity and low ATP binding. Mutant enzyme His-K159L has no blunt end ligation activity, no nick joining activity, no ATP binding, no DNA binding, and no AMP-dependent activity	Tequatrovirus T4

Organism

Organism	UniProt	Comment	Textmining
Tequatrovirus T4	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m	-	Tequatrovirus T4	AMP + diphosphate + (deoxyribonucleotide)n+m	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)