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Literature summary extracted from

  • Marie-Claire, C.; Ruffet, E.; Antonczak, S.; Beaumont, A.; O'Donohue, M.; Roques, B.P.; Fournie-Zaluski, M.C.
    Evidence by site-directed mutagenesis that arginine 203 of thermolysin and arginine 717 of neprilysin (neutral endopeptidase) play equivalent critical roles in substrate hydrolysis and inhibitor binding (1997), Biochemistry, 36, 13938-13945.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.27 cloned in Bacillus subtilis DB117, plasmids subcloned in Escherichia coli Bacillus thermoproteolyticus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.27
-
Bacillus thermoproteolyticus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.27 D170A site-directed mutagenesis Bacillus thermoproteolyticus
3.4.24.27 R203M site-directed mutagenesis Bacillus thermoproteolyticus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.27 phosphoramidon
-
Bacillus thermoproteolyticus
3.4.24.27 Retrothiorphan
-
Bacillus thermoproteolyticus
3.4.24.27 thiorphan
-
Bacillus thermoproteolyticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.27 0.2
-
leucine enkephalin pH 6.8, 37°C, wild-type Bacillus thermoproteolyticus
3.4.24.27 0.24
-
leucine enkephalin pH 6.8, 37°C, mutant D170A Bacillus thermoproteolyticus
3.4.24.27 0.24
-
leucine enkephalin pH 6.8, 37°C, mutant R203M Bacillus thermoproteolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.27 Ca2+ contains 4 structural calcium ions Bacillus thermoproteolyticus
3.4.24.27 Zn2+ zinc-metallopeptidase Bacillus thermoproteolyticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.27 36000
-
Western blot Bacillus thermoproteolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.27 Bacillus thermoproteolyticus
-
Rokko
-
3.4.24.27 Bacillus thermoproteolyticus Rokko
-
Rokko
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.27 wild-type and mutated thermolysin Bacillus thermoproteolyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.27 leucine enkephalin + H2O
-
Bacillus thermoproteolyticus ?
-
?
3.4.24.27 leucine enkephalin + H2O
-
Bacillus thermoproteolyticus Rokko ?
-
?
3.4.24.27 [3H]leucine enkephalin + H2O
-
Bacillus thermoproteolyticus ?
-
?
3.4.24.27 [3H]leucine enkephalin + H2O
-
Bacillus thermoproteolyticus Rokko ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.27 0.083
-
leucine enkephalin pH 6.8, 37°C, mutant R203M Bacillus thermoproteolyticus
3.4.24.27 2.94
-
leucine enkephalin pH 6.8, 37°C, mutant D170A Bacillus thermoproteolyticus
3.4.24.27 1555
-
leucine enkephalin pH 6.8, 37°C, wild-type Bacillus thermoproteolyticus
3.4.24.27 1560
-
leucine enkephalin pH 6.8, 37°C, wild-type Bacillus thermoproteolyticus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.24.27 0.00006
-
phosphoramidon pH 6.8, 37°C, wild-type Bacillus thermoproteolyticus
3.4.24.27 0.0008
-
Retrothiorphan pH 6.8, 37°C, wild-type Bacillus thermoproteolyticus
3.4.24.27 0.0016
-
thiorphan pH 6.8, 37°C, wild-type Bacillus thermoproteolyticus
3.4.24.27 0.0033
-
thiorphan pH 6.8, 37°C, mutant D170A Bacillus thermoproteolyticus
3.4.24.27 0.0047
-
phosphoramidon pH 6.8, 37°C, mutant R203M Bacillus thermoproteolyticus
3.4.24.27 0.16
-
thiorphan pH 6.8, 37°C, mutant R203M Bacillus thermoproteolyticus
3.4.24.27 0.16
-
Retrothiorphan pH 6.8, 37°C, mutant R203M Bacillus thermoproteolyticus