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Literature summary for 3.4.23.24 extracted from

  • Remold, H.; Fasold, H.; Staib, F.
    Purification and characterization of a proteolytic enzyme from Candida albicans (1968), Biochim. Biophys. Acta, 167, 399-406.
    View publication on PubMed

General Stability

General Stability Organism
Enzyme gradually loses activity by standing in solution in the cold or in the frozen state Candida albicans
Unstable to lyophilization Candida albicans
unstable to repeated freezing and thawing Candida albicans

Inhibitors

Inhibitors Comment Organism Structure
additional information heavy metal ions; p-bromophenacyl bromide; SH-blocking reagents Candida albicans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
Candida albicans, gel filtration Candida albicans

Organism

Organism UniProt Comment Textmining
Candida albicans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Candida albicans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Candida albicans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Albumin + H2O low side-chain specificity, preferential attack on hydrophobic amino acid residues Candida albicans ?
-
?
Oxidized insulin B-chain + H2O low side-chain specificity, preferential attack on hydrophobic amino acid residues Candida albicans ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2
-
-
Candida albicans