Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
purified enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 9.2 mg/ml protein in 20 mM acetate, pH 6.0, and 20 mM NaCl, with 0.002 ml of reservoir solution containing 0.2 M NH4NO3 and 15% PEG 3350, equilibration over 0.6 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.6 A resolution | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | complete inhibition at 50 mM | Homo sapiens | |
Zn2+ | complete inhibition at 50 mM | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no significant inhibitory effect of cobalt, nickel or magnesium at 50 mM concentration | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O00584 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | N-linked glycoprotein, enzyme activity is independent of glycosylation, deglycosylation by EndoH leaving one N-acetyl glucosamine residue at each of the N-glycosylation sites | Homo sapiens |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme by metal affinity chromatography, deglycosylation, concanavalin A affinity chromatography and gel filtration | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Homo sapiens | - |
white matter | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | substrate is yeast RNA | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RNase T2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.6 | 6 | assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans, its structure shows a typical fold for members of the T2 RNase family with seven alpha-helices and eight beta-strands constituting an alpha+beta motif, as most of the central anti-parallel beta-sheet is clearly separated in the sequence from the helical parts. The alpha + beta core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences | Homo sapiens |
malfunction | mutations in the gene of human enzyme RNase T2 are associated with white matter disease of the human brain showing bilateral temporal lobe cysts and multifocal white matter lesions which lead to psychomotor impairments,spasticity and epilepsy | Homo sapiens |
additional information | enzyme mode of action independent of its enzymatic activity, overview. The enzyme has four disulfide bridges, connecting cysteine residues 48/55, 75/121, 184/241 and 202/213, its catalytic site comprises residues His65, His113, Glu114, Lys117 and His118 | Homo sapiens |