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Literature summary for 3.4.22.40 extracted from

  • OFarrell, P.A.; Joshua-Tor, L.
    Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure (2007), Biochem. J., 401, 421-428.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli, mutant generation described Saccharomyces cerevisiae

Crystallization (Commentary)

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

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

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
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Purification (Commentary)

Purification (Comment) Organism
gel filtration Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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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 and Products (Substrate)

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
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Synonyms

Synonyms Comment Organism
BH protein
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Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharomyces cerevisiae