Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli, mutant generation described | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
hanging-drop method, structure and catalytic site of yeast bleomycin hydrolase indicated, structural changes at the active site of mutant variants shown, data collection, refinements and structural alignments between wild-type and mutant variants indicated | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
H369A | structural and catalytic effects of mutations shown | Saccharomyces cerevisiae |
H369L | structural and catalytic effects of mutations shown | Saccharomyces cerevisiae |
N392A | structural and catalytic effects of mutations summarized | Saccharomyces cerevisiae |
N392L | structural and catalytic effects of mutations shown | Saccharomyces cerevisiae |
N392V | structural and catalytic effects of mutations shown | Saccharomyces cerevisiae |
Q67E | structural and catalytic effects of mutations indicated | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q01532 | mutant yBH strains and wild-type, features of the catalytic site of bleomycin hydrolase analyzed by mutagenesis of catalytic site residues | - |
Purification (Comment) | Organism |
---|---|
gel filtration | Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
all analyzed mutants compromised in catalytic activity, replacement of the active-site asparagine with alanine, valine or leucine results in destabilization of the histidine side chain and the role of the asparagine residue in correctly positioning the histidine for catalysis, replacement of the histidine with alanine or leucine destabilizes asparagine position | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Arg-7-amido-4-methylcoumarin + H2O | protease activity of mutant variants determined using substrate concentrations ranging from 0 to 0.125 mM | Saccharomyces cerevisiae | L-Arg + 7-amino-4-methylcoumarin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BH protein | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharomyces cerevisiae |