3.4.21.66: Thermitase
This is an abbreviated version!
For detailed information about Thermitase, go to the full flat file.
Word Map on EC 3.4.21.66
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3.4.21.66
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subtilisins
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3.4.21.14
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carlsberg
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subtilisin-like
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subtilases
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subtilisin-type
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eglin-c
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biotechnology
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analysis
- 3.4.21.66
- subtilisins
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3.4.21.14
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carlsberg
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subtilisin-like
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subtilases
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subtilisin-type
- eglin-c
- biotechnology
- analysis
Reaction
Hydrolysis of proteins, including collagen =
Synonyms
Alkaline protease, EC 3.4.21.14, EC 3.4.4.16, PLLA-degrading enzyme, PrlA, Proteinase, Thermoactinomyces vulgaris serine, proteolysin, Thermoactinomyces vulgaris serine proteinase, Thermophilic Streptomyces serine proteinase, thermostable serine protease
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.66 - Thermitase
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REACTION DIAGRAM
Anionic protease + H2O
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at pH 8 or 6 and 25°C or 4°C completely hydrolyzed
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Benzyloxycarbonyl-L-Ala-L-Ala-L-Leu 4-nitroanilide + H2O
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Carbobenzoxy-alanine 4-nitrophenyl ester + H2O
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Streptomyces rectus var. proteolyticus
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Cry11A endotoxin + H2O
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substrate from Bacillus thuringiensis ssp. israelensis, enzyme hydrolyzes the I28-A29 bond. At increasing concentration of enzyme, additionally lysis of M71-E72 bond
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N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
oxidized insulin B chain + H2O
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peptidolytic activity, primary cleavage site of proteolysin is located between Ala14 and Leu15. Prolonged incubation of 24 h reveals additional cleavage sites after Phe1, Asn3, Gln4, Leu17, Cys19, Phe24, Phe25, Tyr25, and Lys29, which shows that proteolysin has a relaxed cleavage site specificity
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Urea-denatured hemoglobin + H2O
Hydrolyzed urea-denatured hemoglobin
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N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
amidolytic activity
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N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
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N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
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N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
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weak activity
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proteolytic activities of cell extracts and purified enzyme samples are monitored on 5% skim milk-LB agar plates or by azocasein assey
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additional information
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proteolytic activities of cell extracts and purified enzyme samples are monitored on 5% skim milk-LB agar plates or by azocasein assey
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additional information
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the enzyme degrades poly(L-lactide) and is a serine protease
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additional information
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a thermostable endo-protease with the ability to convert various food relevant substrates into low-molecular weight peptides, endo-catalytic activity
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additional information
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a thermostable endo-protease with the ability to convert various food relevant substrates into low-molecular weight peptides, endo-catalytic activity
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additional information
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the enzyme degrades poly(L-lactide) and is a serine protease
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additional information
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thermitase is characterized by a free cysteine residue near the active site. The enzyme has a preference for large uncharged residues in S1 and S4 (secondary binding pocket). S1S4 binding sites are rather flat, which may explain broad specificity of the enzyme
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additional information
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at the active site serine and histidine, cysteine and methionine are essential for activity
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additional information
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substrate specificity with proteins, amino acid esters, fatty acid esters and amino acid 4-nitroanilides
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additional information
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thermitase has 5 subsites at the S-site of its active center
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