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Literature summary for 3.4.21.19 extracted from

  • Stennicke, H.R.; Birktoft, J.J.; Breddam, K.
    Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus (1996), Protein Sci., 5, 2266-2275.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Streptomyces griseus

Protein Variants

Protein Variants Comment Organism
H199V change in the substrate preference, with a 16fold increase in the ratio of turnover number to Km-value with substrates with Phe in P1, and a 20fold increase with substrates with Glu in P1. Substitution of His199 by anything except Val completely abolishes the production of mature enzyme Streptomyces griseus
H228A change in substrate specificity, i.e., a slight increase in the ratio of turnover-number to Km-value for the substrate with Asp and a more than 300-fold increase in this ratio when P1 substituent is Ala Streptomyces griseus
S216A about 7.5fold increase in Km-value for hydrolysis of succinyl-Ala-Ala-Pro-Glu-p-nitroanilide compared to the wild-type enzyme Streptomyces griseus
S216G about 7.5fold increase in Km-value for hydrolysis of succinyl-Ala-Ala-Pro-Glu-p-nitroanilide compared to the wild-type enzyme Streptomyces griseus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.026
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant H228A Streptomyces griseus
0.045
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide wild-type enzyme Streptomyces griseus
0.27
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant H199V Streptomyces griseus
0.33
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant S216A Streptomyces griseus
0.34
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant H216G Streptomyces griseus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18263
-
x * 18263, amino acid sequence Streptomyces griseus

Organism

Organism UniProt Comment Textmining
Streptomyces griseus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information distinct preference for Glu, characterization of the S1 binding site Streptomyces griseus ?
-
?
p-aminobenzoyl-Ala-Phe-Ala-Phe-Glu-Val-Phe-Tyr(NO2)-Asp + H2O
-
Streptomyces griseus p-aminobenzoyl-Ala-Phe-Ala-Phe-Glu + Val-Phe-Tyr(NO2)-Asp
-
?
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide + H2O
-
Streptomyces griseus succinyl-Ala-Ala-Pro-Glu + p-nitroaniline
-
?

Subunits

Subunits Comment Organism
? x * 18263, amino acid sequence Streptomyces griseus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
16.7
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant H199V Streptomyces griseus
18.3
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant S216A Streptomyces griseus
21.7
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant H228A Streptomyces griseus
38.3
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide wild-type enzyme Streptomyces griseus
63.3
-
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide mutant H216G Streptomyces griseus