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Literature summary extracted from

  • Shiraki, K.; Norioka, S.; Li, S.; Yokota, K.; Sakiyama, F.
    Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease,Achromobacter protease I (2002), Eur. J. Biochem., 269, 4152-4158.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.50 H210/W169F the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 8.6% of the wild-type ratio Achromobacter lyticus
3.4.21.50 H210A the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 80% of the wild-type ratio Achromobacter lyticus
3.4.21.50 H210A/W169A the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 0.25% of the wild-type ratio Achromobacter lyticus
3.4.21.50 H210K the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 0.02% of the wild-type ratio Achromobacter lyticus
3.4.21.50 H210S the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 1.7fold higher than the wild-type ratio Achromobacter lyticus
3.4.21.50 W169A the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate 0.5% of the wild-type ratio Achromobacter lyticus
3.4.21.50 W169F the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 43% of the wild-type ratio Achromobacter lyticus
3.4.21.50 W169H the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 9% of the wild-type ratio Achromobacter lyticus
3.4.21.50 W169L the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 25% of the wild-type ratio Achromobacter lyticus
3.4.21.50 W169V the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 6% of the wild-type ratio Achromobacter lyticus
3.4.21.50 W169Y the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 43% of the wild-type ratio Achromobacter lyticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.50 Achromobacter lyticus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.50 tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
-
 Achromobacter lyticus tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.50 Achromobacter protease I
-
 Achromobacter lyticus
3.4.21.50 API
-
 Achromobacter lyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.50 8 9 mutant enzyme H210S, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin Achromobacter lyticus
3.4.21.50 9 10 mutant enzyme W169V, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin Achromobacter lyticus
3.4.21.50 9.5
-
 wild-type enzyme, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin Achromobacter lyticus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.50 8 10 pH 8.0: about 40% of maximal activity, pH 10.0: about 95% of maximal activity, wild-type enzyme, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin Achromobacter lyticus