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Literature summary for 3.1.3.73 extracted from

  • Watkins, H.A.; Baker, E.N.
    Structural and functional characterisation of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis (2010), J. Bacteriol., 192, 2878-2886.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
maltose binding protein fusion protein expressed in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
N-terminal domain (RNase activity), sitting drop method Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.07
-
alpha-ribazole 5'-phosphate
-
Mycobacterium tuberculosis
5.5
-
p-nitrophenol phosphate full length protein Mycobacterium tuberculosis
13.6
-
p-nitrophenol phosphate maltose binding protein fusion protein Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WLH5
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose affinity chromatography, gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-ribazole 5'-phosphate + H2O
-
Mycobacterium tuberculosis alpha-ribazole + phosphate
-
?
alpha-ribazole 5'-phosphate + H2O
-
Mycobacterium tuberculosis H37Rv alpha-ribazole + phosphate
-
?
p-nitrophenyl phosphate + H2O
-
Mycobacterium tuberculosis p-nitrophenol + phosphate
-
?
p-nitrophenyl phosphate + H2O
-
Mycobacterium tuberculosis H37Rv p-nitrophenol + phosphate
-
?

Synonyms

Synonyms Comment Organism
alpha-ribazole phosphatase bifunctional enzyme: RNase H activity Mycobacterium tuberculosis
CobC
-
Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
substrate p-nitrophenyl phosphate Mycobacterium tuberculosis