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Literature summary for 6.5.1.3 extracted from

  • Ho, C.K.; Wang, L.K.; Lima, C.D.; Shuman, S.
    Structure and mechanism of RNA ligase (2004), Structure, 12, 327-339.
    View publication on PubMed
Search for more literature for 6.5.1.3

Cloned(Commentary)

Cloned (Comment) Organism
-
 Tequatrovirus T4

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

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

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4 P32277
-
-

Purification (Commentary)

Purification (Comment) Organism
produced in Escherichia coli Tequatrovirus T4

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Rnl2
-
 Tequatrovirus T4
T4 RNA ligase 2
-
 Tequatrovirus T4

pH Optimum

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