Literature summary extracted from

Ho, C.K.; Wang, L.K.; Lima, C.D.; Shuman, S.
Structure and mechanism of RNA ligase (2004), Structure, 12, 327-339.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
6.5.1.3	-	Tequatrovirus T4

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
6.5.1.3	crystal structure of the ligase domain with AMP bound at the active site, space group P2(1)2(1)2, a = 57.72 A, b = 89.89 A, c = 47.74 A	Tequatrovirus T4

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
6.5.1.3	ATP + (ribonucleotide)n + (ribonucleotide)m	Tequatrovirus T4	-	AMP + diphosphate + (ribonucleotide)n+m	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.5.1.3	Tequatrovirus T4	P32277	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
6.5.1.3	produced in Escherichia coli	Tequatrovirus T4

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6.5.1.3	ATP + (ribonucleotide)n + (ribonucleotide)m	-	Tequatrovirus T4	AMP + diphosphate + (ribonucleotide)n+m	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
6.5.1.3	Rnl2	-	Tequatrovirus T4
6.5.1.3	T4 RNA ligase 2	-	Tequatrovirus T4

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5.1.3	6.5	-	adenylyltransferase activity	Tequatrovirus T4
6.5.1.3	9	9.5	-	Tequatrovirus T4

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Release 2023.1 (January 2023)