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Literature summary for 3.4.21.62 extracted from

  • Tang, H.; Zhang, J.; Shi, K.; Aihara, H.; Du, G.
    Insight into subtilisin E-S7 cleavage pattern based on crystal structure and hydrolysates peptide analysis (2019), Biochem. Biophys. Res. Commun., 512, 623-628 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.62

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, mixing of 30 mg/ml protein in 30 mM Tris-HCl, pH 7.4, and 150 mM NaCl, with 0.15 M ammonium sulfate, 15% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.0, X-ray diffraction structure determination and analysis at 1.83-1.90 A, molecular replacement and modeling Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
S221C site-directed mutagenesis, mutation of the critical catalytic residue Ser221 of SES7 to a cysteine to avoid protease self-digestion Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
angiotensin-converting enzyme IC50 is 0.067 mg/ml Bacillus subtilis
neurolysin IC50 is 0.263 mg/ml Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis JN-S7
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme propeptide is cleaved to the mature form Bacillus subtilis

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O SES7 clleavage pattern, overview Bacillus subtilis ?
-
 ?
alpha-casein + H2O SES7 clleavage pattern, overview Bacillus subtilis JN-S7 ?
-
 ?
beta-casein + H2O SES7 clleavage pattern, overview Bacillus subtilis ?
-
 ?
beta-casein + H2O SES7 clleavage pattern, overview Bacillus subtilis JN-S7 ?
-
 ?
additional information the wild-type enzyme performs autoproteolysis, while the enzyme mutant S221C does not. The cleavage patterns of SES7 is determined by hydrolysates peptide profile, it prefers amino acids Q, T, P, or L at P3, P, V and Q at P2, K, L, N, Q, or F at P1, and F, S, or A at P1' Bacillus subtilis ?
-
 ?
additional information the wild-type enzyme performs autoproteolysis, while the enzyme mutant S221C does not. The cleavage patterns of SES7 is determined by hydrolysates peptide profile, it prefers amino acids Q, T, P, or L at P3, P, V and Q at P2, K, L, N, Q, or F at P1, and F, S, or A at P1' Bacillus subtilis JN-S7 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 28800, recombinant mature enzyme, SDS-PAGE, x * 37400, proenzyme, SDS-PAGE Bacillus subtilis

Synonyms

Synonyms Comment Organism
SES7
-
 Bacillus subtilis
subtilisin E-S7
-
 Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Bacillus subtilis

General Information

General Information Comment Organism
evolution enzyme subtilisin E-S7 (SES7) has 3 amino acids different from subtilisin E (1SCJ): S85A, T130S, and T162S Bacillus subtilis