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Literature summary 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)

EC Number Cloned (Comment) Organism
3.1.3.73 maltose binding protein fusion protein expressed in Escherichia coli Mycobacterium tuberculosis
3.1.26.4 expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.73 N-terminal domain (RNase activity), sitting drop method Mycobacterium tuberculosis
3.1.26.4 fusion protein of maltose binding protein and the N-terminal RNase H domain, to 2.2.5 A resolution. Protein is monomeric in solution but associates in the crystal to form a dimer Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.4 additional information fusion protein of maltose binding protein and the N-terminal RNase H domain shows RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. The full-length protein has additional CobC activity Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.73 1.07
-
 alpha-ribazole 5'-phosphate
-
 Mycobacterium tuberculosis
3.1.3.73 5.5
-
 p-nitrophenol phosphate full length protein Mycobacterium tuberculosis
3.1.3.73 13.6
-
 p-nitrophenol phosphate maltose binding protein fusion protein Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.73 Mycobacterium tuberculosis P9WLH5
-
-
3.1.26.4 Mycobacterium tuberculosis P9WLH5 bifunctional protein, the N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with alpha-ribazole phosphatase CobC
-
3.1.26.4 Mycobacterium tuberculosis H37Rv P9WLH5 bifunctional protein, the N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with alpha-ribazole phosphatase CobC
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.73 alpha-ribazole 5'-phosphate + H2O
-
 Mycobacterium tuberculosis alpha-ribazole + phosphate
-
 ?
3.1.3.73 alpha-ribazole 5'-phosphate + H2O
-
 Mycobacterium tuberculosis H37Rv alpha-ribazole + phosphate
-
 ?
3.1.3.73 p-nitrophenyl phosphate + H2O
-
 Mycobacterium tuberculosis p-nitrophenol + phosphate
-
 ?
3.1.3.73 p-nitrophenyl phosphate + H2O
-
 Mycobacterium tuberculosis H37Rv p-nitrophenol + phosphate
-
 ?
3.1.26.4 RNA-DNA duplex + H2O substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain Mycobacterium tuberculosis ?
-
 ?
3.1.26.4 RNA-DNA duplex + H2O substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain Mycobacterium tuberculosis H37Rv ?
-
 ?
3.1.26.4 RNA-RNA duplex + H2O substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain Mycobacterium tuberculosis ?
-
 ?
3.1.26.4 RNA-RNA duplex + H2O substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.73 alpha-ribazole phosphatase bifunctional enzyme: RNase H activity Mycobacterium tuberculosis
3.1.3.73 CobC
-
 Mycobacterium tuberculosis
3.1.26.4 Rv2228c
-
 Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.73 4
-
 substrate p-nitrophenyl phosphate Mycobacterium tuberculosis