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Literature summary for 3.4.24.27 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Bacillus thermoproteolyticus

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
phosphoramidon
-
Bacillus thermoproteolyticus
Retrothiorphan
-
Bacillus thermoproteolyticus
thiorphan
-
Bacillus thermoproteolyticus

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bacillus thermoproteolyticus
-
Rokko
-
Bacillus thermoproteolyticus Rokko
-
Rokko
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Ki Value [mM]

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