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Literature summary for 3.4.21.89 extracted from

  • Matsumi, R.; Atomi, H.; Imanaka, T.
    Identification of the amino acid residues essential for proteolytic activity in an archaeal signal peptide peptidase (2006), J. Biol. Chem., 281, 10533-10539.
    View publication on PubMed
Search for more literature for 3.4.21.89

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Thermococcus kodakarensis

Protein Variants

Protein Variants Comment Organism
D215A Vmax is 1.8fold lower than wild-type value, kcat is 1.8 fold lower than wild-type enzyme Thermococcus kodakarensis
D277A Vmax is 1.6fold higher than wild-type value, kcat is 1.6fold higher than wild-type enzyme Thermococcus kodakarensis
E226A Vmax is 1.35fold higher than wild-type value, kcat is 1.3fold higher than wild-type enzyme Thermococcus kodakarensis
E227A Vmax is is nearly identical to wild-type value, kcat nearly identical to wild-type enzyme Thermococcus kodakarensis
H191A Vmax is 1.84fold lower than wild-type value, kcat is 1.9fold lower than wild-type enzyme Thermococcus kodakarensis
K150A Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme Thermococcus kodakarensis
K209A Vmax is 1.7fold lower than wild-type value, kcat is 1.8fold lower than wild-type enzyme Thermococcus kodakarensis
additional information a truncated protein without the N-terminal 54 residues and putative transmembrane domain, exhibits high peptidase activity, and is used as the wild-type protein Thermococcus kodakarensis
R221A Vmax is 7.8fold lower than wild-type value, kcat is 8fold lower than wild-type enzyme Thermococcus kodakarensis
R250A Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme Thermococcus kodakarensis
S128A Vmax is 6.9 fold higher than wild-type value, kcat is 6.2fold higher than wild-type enzyme Thermococcus kodakarensis
S184A Vmax is 4fold lower than wild-type value, kcat is 4fold lower than wild-type enzyme Thermococcus kodakarensis
Y165A Vmax is 2.3fold higher than wild-type value, kcat is 2.3fold higher than wild-type enzyme Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Phe-4-methylcoumaryl-7-amide + H2O
-
 Thermococcus kodakarensis Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme R221A Thermococcus kodakarensis
4
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme S184A Thermococcus kodakarensis
8.6
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme H191A Thermococcus kodakarensis
8.8
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme D215A Thermococcus kodakarensis
9.1
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme K209A Thermococcus kodakarensis
16
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme E227A Thermococcus kodakarensis
16
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, wild-type enzyme Thermococcus kodakarensis
21
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme E226A Thermococcus kodakarensis
23
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme K150A Thermococcus kodakarensis
23
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme R250A Thermococcus kodakarensis
25
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme D277A Thermococcus kodakarensis
37
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme Y165A Thermococcus kodakarensis
110
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme S128A Thermococcus kodakarensis