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 |
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 |
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 |
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 |
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 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.73 | amylose affinity chromatography, gel filtration | Mycobacterium tuberculosis |
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 | ? | - |
? |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.73 | 4 | - |
substrate p-nitrophenyl phosphate | Mycobacterium tuberculosis |