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Literature summary extracted from

  • Liu, F.; Zhao, Z.S.; Ren, Y.; Cheng, G.; Tang, X.F.; Tang, B.
    Autocatalytic activation of a thermostable glutamyl endopeptidase capable of hydrolyzing proteins at high temperatures (2016), Appl. Microbiol. Biotechnol., 100, 10429-10441 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.19 a proform that contains a 61-amino acid N-terminal propeptide and a 218-amino acid mature domain are expressed in Escherichia coli BL21(DE3) cells Thermoactinomyces sp. CDF

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.19 S168C the mutant does not show proteolytic and azocaseinolytic activity Thermoactinomyces sp. CDF

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.19 EDTA partial inhibition Thermoactinomyces sp. CDF
3.4.21.19 phenylmethylsulfonyl fluoride partial inhibition Thermoactinomyces sp. CDF
3.4.21.19 SDS partial inhibition. The enzyme is resistant to the SDS treatment in the presence of 10 mM CaCl2 Thermoactinomyces sp. CDF

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.19 Ca2+ Ca2+ contributes to the thermostability of the enzyme Thermoactinomyces sp. CDF
3.4.21.19 Cu2+ strong inhibition Thermoactinomyces sp. CDF
3.4.21.19 additional information the enzyme activity is not affected by Ca2+ and Mg2+ Thermoactinomyces sp. CDF
3.4.21.19 Zn2+ strong inhibition Thermoactinomyces sp. CDF

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.19 additional information Thermoactinomyces sp. CDF the enzyme specifically hydrolyzes peptide bonds formed by alpha-carboxyl groups of Glu and Asp residues. Glu-Xaa bonds are cleaved much more efficiently than Asp-Xaa bonds ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.19 Thermoactinomyces sp. CDF
-
 CCTCC AB206328
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.19 Ni2+-charged chelating Sepharose column chromatography and Superdex S200 gel filtration Thermoactinomyces sp. CDF

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.19 azocasein + H2O
-
 Thermoactinomyces sp. CDF ?
-
 ?
3.4.21.19 beta-casein + H2O
-
 Thermoactinomyces sp. CDF ?
-
 ?
3.4.21.19 Bovine serum albumin + H2O
-
 Thermoactinomyces sp. CDF ?
-
 ?
3.4.21.19 additional information the enzyme specifically hydrolyzes peptide bonds formed by alpha-carboxyl groups of Glu and Asp residues. Glu-Xaa bonds are cleaved much more efficiently than Asp-Xaa bonds Thermoactinomyces sp. CDF ?
-
 ?
3.4.21.19 ovalbumin + H2O
-
 Thermoactinomyces sp. CDF ?
-
 ?
3.4.21.19 Oxidized insulin B-chain + H2O cleavage occurs at Glu13-Ala14 and Glu21-Arg22 Thermoactinomyces sp. CDF ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.19 ? x * 26000, SDS-PAGE Thermoactinomyces sp. CDF

Synonyms

EC Number Synonyms Comment Organism
3.4.21.19 GSE
-
 Thermoactinomyces sp. CDF

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.19 85
-
-
 Thermoactinomyces sp. CDF

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.19 60 70 in the presence of 10 mM CaCl2, the enzyme does not show loss of activity after incubation at 60°C for 6 h and retains approximately 90% of its original activity after incubation at 70°C for 6 h Thermoactinomyces sp. CDF

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.19 8.5
-
-
 Thermoactinomyces sp. CDF

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.19 6 10 the mature form has high azocaseinolytic activity over a broad pH range of pH 6.0-10.0 Thermoactinomyces sp. CDF