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Literature summary for 3.1.21.10 extracted from

  • Nautiyal, A.; Rani, P.S.; Sharples, G.J.; Muniyappa, K.
    Mycobacterium tuberculosis RuvX is a Holliday junction resolvase formed by dimerisation of the monomeric YqgF nuclease domain (2016), Mol. Microbiol., 100, 656-674 .
    View publication on PubMed
Search for more literature for 3.1.21.10

Cloned(Commentary)

Cloned (Comment) Organism
-
 Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
D28N mutation reduced its ability to cleave Holliday junction DNA Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme requires a divalent cation for Holliday junction cleavage (typically Mg2+ or Mn2+), but not for Holliday junction binding activity Mycobacterium tuberculosis
Mn2+ the enzyme requires a divalent cation for Holliday junction cleavage (typically Mg2+ or Mn2+), but not for Holliday junction binding activity Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 gel filtration Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGV7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Subunits

Subunits Comment Organism
homodimer
-
 Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
RuvX Holliday junction resolvase formed by dimerisation of the monomeric YqgF nuclease domain Mycobacterium tuberculosis

Expression

Organism Comment Expression
Mycobacterium tuberculosis expression is induced in response to DNA damage up