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Literature summary extracted from

  • Qoura, F.; Kassab, E.; Reisse, S.; Antranikian, G.; Brueck, T.
    Characterization of a new, recombinant thermo-active subtilisin-like serine protease derived from Shewanella arctica (2015), J. Mol. Catal. B, 116, 16-23 .
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.62 aprotonin 10% activation at 1 mM Shewanella frigidimarina
3.4.21.62 leupeptin 15% activation at 1 mM Shewanella frigidimarina
3.4.21.62 phosphoramidon 20% activation at 1 mM Shewanella frigidimarina

Application

EC Number Application Comment Organism
3.4.21.62 detergent enzyme SaP can be useful for industrial application operating over a broad temperature range, such as household detergent formulations Shewanella frigidimarina

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.62 gene ORF2, from a gene library of the psychrophilic bacterium Shewanella arctica, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain XLOLR and Tuner (DE3) pLacl from vector pET Blue-1, method optimization Shewanella frigidimarina

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.62 acetonitril high concentrations of acetonitrile significantly decrease the enzyme activity by over 60%, most likely due to disrupting the enzyme structural integrity Shewanella frigidimarina
3.4.21.62 antipain 35% inhibition at 1 mM, 95% at 5 mM Shewanella frigidimarina
3.4.21.62 chymostatin complete inhibition at 1 mM Shewanella frigidimarina
3.4.21.62 E-64 37% inhibition at 5 mM Shewanella frigidimarina
3.4.21.62 additional information the enzyme activity is not affected by various metal ions or non-specific protease inhibitors, e.g. bestatin, leupeptin, or pefabloc SC Shewanella frigidimarina
3.4.21.62 PMSF complete inhibition at 10 mM, no effect at 0.01 mM Shewanella frigidimarina
3.4.21.62 Urea high concentrations (6 M) of urea significantly decrease the enzyme activity by over 60%, most likely due to disrupting the enzyme structural integrity Shewanella frigidimarina

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.62 additional information
-
 additional information Michaelis-Menten kinetics, Km is 0.175% w/v Shewanella frigidimarina

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.62 additional information the enzyme contains a 4.4 kDa/38 amino-acid signal sequence Shewanella frigidimarina
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.62 Shewanella frigidimarina A0A0B6XK99
-
-
3.4.21.62 Shewanella frigidimarina DSM 16509 A0A0B6XK99
-
-
3.4.21.62 Shewanella frigidimarina JCM 14208 A0A0B6XK99
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.62 recombinant enzyme from Escherichia coli to homogeneity Shewanella frigidimarina

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.62 0.52
-
 purified recombinant enzyme, pH 8.0, 60°C Shewanella frigidimarina

Storage Stability

EC Number Storage Stability Organism
3.4.21.62 -20°C, purified recombinant enzyme, 55% activity remaining after 35 days Shewanella frigidimarina
3.4.21.62 -80°C, purified recombinant enzyme, 50% activity remaining after 35 days Shewanella frigidimarina

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.62 casein + H2O
-
 Shewanella frigidimarina ?
-
 ?
3.4.21.62 casein + H2O
-
 Shewanella frigidimarina DSM 16509 ?
-
 ?
3.4.21.62 casein + H2O
-
 Shewanella frigidimarina JCM 14208 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.62 ? x * 67000, about, sequence calculation Shewanella frigidimarina
3.4.21.62 More in-silico structural modelling and analysis Shewanella frigidimarina

Synonyms

EC Number Synonyms Comment Organism
3.4.21.62 ORF2
-
 Shewanella frigidimarina
3.4.21.62 SAP
-
 Shewanella frigidimarina
3.4.21.62 thermo-active subtilisin-like serine protease
-
 Shewanella frigidimarina

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.62 60
-
 recombinant enzyme Shewanella frigidimarina

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.21.62
-
 80 activity range, over 20% of maximal activity within this range Shewanella frigidimarina

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.62 40
-
 purified recombinant enzyme, 45 h, 50% activity remaining, 90% remaning after 10 h Shewanella frigidimarina
3.4.21.62 55
-
 purified recombinant enzyme, 3 h, 35-40% activity remaining, inactivation after 7 h Shewanella frigidimarina
3.4.21.62 70
-
 purified recombinant enzyme, 1.5 h, 50% activity remaining, 15% after 2 h Shewanella frigidimarina
3.4.21.62 80 90 purified recombinant enzyme, inactivation within 30 min Shewanella frigidimarina

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.62 5.186
-
 casein recombinant enzyme, pH 8.0, 60°C Shewanella frigidimarina

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.62 8
-
 recombinant enzyme Shewanella frigidimarina

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.62 6 10 activity range, over 65% of maximal activity within this range Shewanella frigidimarina

General Information

EC Number General Information Comment Organism
3.4.21.62 additional information initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135 Shewanella frigidimarina

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.21.62 0.07114
-
 casein recombinant enzyme, pH 8.0, 60°C Shewanella frigidimarina