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Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.89 D215A Vmax is 1.8fold lower than wild-type value, kcat is 1.8 fold lower than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 D277A Vmax is 1.6fold higher than wild-type value, kcat is 1.6fold higher than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 E226A Vmax is 1.35fold higher than wild-type value, kcat is 1.3fold higher than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 E227A Vmax is is nearly identical to wild-type value, kcat nearly identical to wild-type enzyme Thermococcus kodakarensis
3.4.21.89 H191A Vmax is 1.84fold lower than wild-type value, kcat is 1.9fold lower than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 K150A Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 K209A Vmax is 1.7fold lower than wild-type value, kcat is 1.8fold lower than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 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
3.4.21.89 R221A Vmax is 7.8fold lower than wild-type value, kcat is 8fold lower than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 R250A Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 S128A Vmax is 6.9 fold higher than wild-type value, kcat is 6.2fold higher than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 S184A Vmax is 4fold lower than wild-type value, kcat is 4fold lower than wild-type enzyme Thermococcus kodakarensis
3.4.21.89 Y165A Vmax is 2.3fold higher than wild-type value, kcat is 2.3fold higher than wild-type enzyme Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.89 Thermococcus kodakarensis
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.89 2
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme R221A Thermococcus kodakarensis
3.4.21.89 4
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme S184A Thermococcus kodakarensis
3.4.21.89 8.6
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme H191A Thermococcus kodakarensis
3.4.21.89 8.8
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme D215A Thermococcus kodakarensis
3.4.21.89 9.1
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme K209A Thermococcus kodakarensis
3.4.21.89 16
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme E227A Thermococcus kodakarensis
3.4.21.89 16
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, wild-type enzyme Thermococcus kodakarensis
3.4.21.89 21
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme E226A Thermococcus kodakarensis
3.4.21.89 23
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme K150A Thermococcus kodakarensis
3.4.21.89 23
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme R250A Thermococcus kodakarensis
3.4.21.89 25
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme D277A Thermococcus kodakarensis
3.4.21.89 37
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme Y165A Thermococcus kodakarensis
3.4.21.89 110
-
 Ala-Ala-Phe-4-methylcoumaryl-7-amide 60°C, pH 10.0, mutant enzyme S128A Thermococcus kodakarensis