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Literature summary for 3.4.21.19 extracted from

  • Mil'gotina, E.I.; Voyushina, T.L.; Chestukhina, G.G.
    Glutamyl endopeptidases: structure, function, and practical application (2003), Russ. J. Bioorg. Chem., 29, 511-522.
No PubMed abstract available
Search for more literature for 3.4.21.19

Application

Application Comment Organism
analysis study of structure-function organization of anti-HIV and antitumor proteins MAP30 and GAP31 by limited proteolysis with V8-GSE, enzym may be useful for studying other proteins as well Staphylococcus aureus
synthesis enzyme can be used as catalyst for peptide synthesis in hydrophilic organic solvents with low water content, e.g. acetonitrile, overview Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme is crystallized complexed with substrate Boc-Ala-Ala-Pro-Glu-4-nitroanilide, X-ray structure determination and analysis at 2.0 A resolution Streptomyces griseus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information enzyme is a metalloprotease Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-
Bacillus subtilis
-
 enzyme possesses Cys at position 193 instead of highly conserved Gly, the most conserved residue of the trypsin enzyme family
-
Staphylococcus aureus
-
-
-
Staphylococcus aureus V8
-
-
-
Streptomyces griseus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Preferential cleavage: Glu-/-, Asp-/- catalytic tetrad of His213, Asp102, Ser195, and Trp214, computer modeling of S1 and S'1 sites of the enzyme's active site Staphylococcus aureus
a
Preferential cleavage: Glu-/-, Asp-/- catalytic triad of His, Asp, and Ser Bacillus subtilis
a
Preferential cleavage: Glu-/-, Asp-/- catalytic triad of His, Asp, and Ser, computer modeling of active site structure, S1-substrate binding site, and substrate binding mechanism Bacillus licheniformis
a
Preferential cleavage: Glu-/-, Asp-/- catalytic triad of His, Asp, and Ser, substrate binding mechanism and structure Streptomyces griseus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus ?
-
 ?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Bacillus licheniformis ?
-
 ?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus V8 ?
-
 ?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus ?
-
 ?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Bacillus licheniformis ?
-
 ?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus V8 ?
-
 ?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus ?
-
 ?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Bacillus licheniformis ?
-
 ?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus ?
-
 ?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Bacillus licheniformis ?
-
 ?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus V8 ?
-
 ?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus ?
-
 ?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Bacillus licheniformis ?
-
 ?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O enzyme also performs acyl-transfer reaction with substrate mimetics Staphylococcus aureus V8 ?
-
 ?
benzyloxycarbonyl-Ala-Ala-Glu-methyl ester + leucine * HCl peptide synthesis Staphylococcus aureus benzyloxycarbonyl-Ala-Ala-Glu-Leu + methanol
-
 ?
benzyloxycarbonyl-Ala-Glu-methyl ester + leucine * HCl peptide synthesis Staphylococcus aureus benzyloxycarbonyl-Ala-Glu-Leu + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Ala-Ala-D-hydroxyalanine peptide synthesis, low activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Ala-Ala-D-hydroxyalanine + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Ala-Ala-hydroxyproline peptide synthesis, lower activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Ala-Ala-hydroxyproline + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Ala-D-hydroxyalanine peptide synthesis, very low activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Ala-D-hydroxyalanine + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyaspartate peptide synthesis, low activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Ala-hydroxyaspartate + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyglutamate peptide synthesis, very low activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Ala-hydroxyglutamate + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyproline peptide synthesis, no activity at 25°C, only low activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Ala-hydroxyproline + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Asp-Gly peptide synthesis, no activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Asp-Gly + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + aspartate peptide synthesis, no activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Asp + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + Glu-Gly peptide synthesis, no activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Glu-Gly + methanol
-
 ?
benzyloxycarbonyl-Asp-methyl ester + glutamate peptide synthesis, no activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Asp-Glu + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Ala-Ala-D-Ala peptide synthesis, low activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Ala-Ala-D-Ala + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Ala-Ala-Pro peptide synthesis, lower activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Ala-Ala-Pro + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Ala-Asp peptide synthesis, no activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Ala-Asp + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Ala-D-Ala peptide synthesis, no activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Ala-D-Ala + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Ala-Glu peptide synthesis, no activity at 25°C, but high activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Ala-Glu + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Ala-Pro peptide synthesis, no activity at 25°C, only low activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Ala-Pro + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Asp-Gly peptide synthesis, no activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Asp-Gly + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Glu-Gly peptide synthesis, no activity at 25°C, but low activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Glu-Gly + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + L-aspartate peptide synthesis, no activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Asp + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + L-glutamate peptide synthesis, no activity at 25°C, but moderate activity at -15°C Bacillus licheniformis benzyloxycarbonyl-Glu-Glu + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + L-tryptophan peptide synthesis Staphylococcus aureus benzyloxycarbonyl-Glu-Trp + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Leu-Gly peptide synthesis Staphylococcus aureus benzyloxycarbonyl-Glu-Leu-Gly + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + leucine peptide synthesis Staphylococcus aureus benzyloxycarbonyl-Glu-Leu + methanol
-
 ?
benzyloxycarbonyl-Glu-methyl ester + Phe-Gly peptide synthesis Staphylococcus aureus benzyloxycarbonyl-Glu-Phe-Gly + methanol
-
 ?
benzyloxycarbonyl-Pro-Leu-Gly-S-CH2-COOH + LAFARAEAFG acylation of peptide fragment by substrate mimetic Staphylococcus aureus benzyloxycarbonyl-PLGLAFARAEAFG + HS-CH2-COOH product formation 55% ?
benzyloxycarbonyl-S-CH2-COOH + LAFARAEAF-hydroxyglycine acylation of peptide fragment by substrate mimetic Staphylococcus aureus benzyloxycarbonyl-LAFARAEAF-hydroxyglycine + HS-CH2-COOH product formation 99% ?
beta-type parvalbumin + H2O from the frog Rana catesbeiana Staphylococcus aureus peptide fragments mass spectrometry for identification ?
bovine hemoglobin + H2O in presence of SDS Staphylococcus aureus peptide fragments peptide mapping, 2 peptide fragments are Leu76-Pro-Gly-Ala-Leu-Ser-Glu82 and Lys94-Leu-His-Val-Asp-Pro-Glu100 ?
hemocyanin + H2O hydrolysis of 2 isozymes of hemocyanin KLH1 and KLH2 from shellfish Megatura crenulata at Glu-Xaa and Asp-Xaa bonds Staphylococcus aureus peptide fragments
-
 ?
additional information no peptide synthesis activity with proline and D-leucine, active in semienzymatic synthesis of human growth hormone Bacillus licheniformis ?
-
 ?
additional information substrate specificity is pH-dependent due to active site His213, peptide synthesizing substrate specificity, no peptide synthesizing activity with benzyloxycarbonyl-Asp-methyl ester Staphylococcus aureus ?
-
 ?
additional information substrate specificity is pH-dependent due to active site His213, peptide synthesizing substrate specificity, no peptide synthesizing activity with benzyloxycarbonyl-Asp-methyl ester Staphylococcus aureus V8 ?
-
 ?
tert-butyloxycarbonyl-Ala-Ala-Pro-Glu-4-nitroanilide + H2O
-
 Streptomyces griseus tert-butyloxycarbonyl-Ala-Ala-Pro-Glu + 4-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
More structural and functional organization, overview, enzyme shows 2 beta-barrels and a C-terminal alpha-helix when complexed with substrate Boc-Ala-Ala-Pro-Glu-4-nitroanilide Streptomyces griseus
More structural and functional rganization, overview Staphylococcus aureus
More structural and functional rganization, overview Bacillus subtilis
More structural and functional rganization, overview Bacillus licheniformis

Synonyms

Synonyms Comment Organism
BL-GSE
-
 Bacillus licheniformis
BS-GSE
-
 Bacillus subtilis
glutamic acid-specific endopeptidase
-
 Staphylococcus aureus
glutamic acid-specific endopeptidase
-
 Bacillus subtilis
glutamic acid-specific endopeptidase
-
 Bacillus licheniformis
glutamic acid-specific endopeptidase
-
 Streptomyces griseus
SG-GSE
-
 Streptomyces griseus
V8 protease
-
 Staphylococcus aureus
V8-GSE
-
 Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 peptide synthesis at -15°C Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3 8
-
 Bacillus licheniformis
9
-
-
 Streptomyces griseus

pI Value

Organism Comment pI Value Maximum pI Value
Staphylococcus aureus 2 ionogenic groups
-
 additional information