EC Number   |
General Information |
Reference |
|---|
   4.6.1.24 | evolution |
the enzyme belongs to the RNase T1 family |
729434 |
| 4.6.1.24 | evolution |
the enzyme belongs to the RNase T1 family, comparison of the amino acid sequences, overview |
729351 |
| 4.6.1.24 | evolution |
the enzyme is a member of the RNase T1 family |
729442 |
| 4.6.1.24 | malfunction |
deletion of gene rng leads to accumulation of 23S rRNA precursors in Escherichia coli |
-, 717985 |
| 4.6.1.24 | metabolism |
binase is involved in phosphate metabolism, low concentrations of extracellular inorganic phosphate induce the expression of phosphate regulon, Pho, genes, as well as the binase gene, binase expression is strongly dependent on a functional PhoP-PhoR two-component system |
717597 |
| 4.6.1.24 | metabolism |
distinct roles of RNase E and RNase G in mRNA decay and tRNA processing, overview |
716898 |
| 4.6.1.24 | more |
analysis of cumulative permeation and skin deposition of negatively charged RNAse T1 using porcine ear skin. RNAse T1 permeation is dependent upon current density,while skin deposition is not. RNAse T1 retains structural integrity and enzymatic function postiontophoresis. RNAse T1 appears to be bound to the epidermis alone |
717913 |
| 4.6.1.24 | more |
comparison of the electrostatic potential of the molecular surfaces of RNase Po1 and RNase T1 shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically, determination of the three-dimensional X-ray structure of RNase Po1 and comparison to that of RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. The base recognition site of RNase T1 consists of Tyr42, Asn43, Asn44, Glu46, Tyr45, and Asn98 and is located in the loop between beta3-4 strands (Asn43, Asn44, Tyr45, Glu46) and in the loop between beta6-7 strands (Asn98). In case of the base recognition site of RNase Po1, the amino acid residues Tyr38, Asn39, Asn40, Phe41, Glu42, and Asn94 correspond to those of RNase T1 |
729351 |
| 4.6.1.24 | more |
comparison with barnase from Bacillus amyloliquefaciens, overview. Mutation in resD leads to a significant decrease in binase production, whereas mutation in spo0A causes its hyperproduction. Expression of binase is possible only in Spo0A-OFF cells |
717597 |
| 4.6.1.24 | more |
comparison with binase from Bacillus pumilus, overview. Barnase expression is strictly dependent on activating Spo0A, the Spo0A protein is a multifunctional regulator that controls stress-related processes, such as sporulation, biofilm formation and cannibalism |
717597 |
