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Literature summary for 3.4.21.62 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
Search for more literature for 3.4.21.62

Activating Compound

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

Application

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

Cloned(Commentary)

Cloned (Comment) Organism
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

Inhibitors Comment Organism Structure
acetonitril high concentrations of acetonitrile significantly decrease the enzyme activity by over 60%, most likely due to disrupting the enzyme structural integrity Shewanella frigidimarina
antipain 35% inhibition at 1 mM, 95% at 5 mM Shewanella frigidimarina
chymostatin complete inhibition at 1 mM Shewanella frigidimarina
E-64 37% inhibition at 5 mM Shewanella frigidimarina
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
PMSF complete inhibition at 10 mM, no effect at 0.01 mM Shewanella frigidimarina
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]

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

Localization

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

Organism

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

pH Range

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

General Information

General Information Comment Organism
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]

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