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Literature summary extracted from

  • Hong, S.J.; Lee, Y.H.; Khan, A.R.; Ullah, I.; Lee, C.; Park, C.K.; Shin, J.H.
    Cloning, expression, and characterization of thermophilic L-asparaginase from Thermococcus kodakarensis KOD1 (2014), J. Basic Microbiol., 54, 500-508.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.1 food industry the acrylamide contents in baked dough were reduced to sixty percent after treatment with recombinant enzyme as compared to the untreated control Thermococcus kodakarensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1 expressed in Escherichia coli BLR(DE3) cells Thermococcus kodakarensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.1 Ca2+ 80% residual activity at 1 mM Thermococcus kodakarensis
3.5.1.1 Co2+ complete inhibition at 1 mM Thermococcus kodakarensis
3.5.1.1 Cu2+ 15% residual activity at 1 mM Thermococcus kodakarensis
3.5.1.1 EDTA 90% residual activity at 1 mM Thermococcus kodakarensis
3.5.1.1 Ni2+ complete inhibition at 1 mM Thermococcus kodakarensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 2.6
-
 L-asparagine at pH 8.0 and 90°C Thermococcus kodakarensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.1 Mg2+ 138% activity at 1 mM Thermococcus kodakarensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.1 37000
-
 2 * 37000, SDS-PAGE Thermococcus kodakarensis
3.5.1.1 71000
-
 gel filtration Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.1 L-asparagine + H2O Thermococcus kodakarensis
-
 L-aspartate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Thermococcus kodakarensis Q5JHT1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1 Ni-NTA column chromatography, and gel filtration Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.1 541.9
-
 crude enzyme, at pH 8.0 and 90°C Thermococcus kodakarensis
3.5.1.1 978.7
-
 after 1.8fold purification, at pH 8.0 and 90°C Thermococcus kodakarensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O
-
 Thermococcus kodakarensis L-aspartate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.1 homodimer 2 * 37000, SDS-PAGE Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 Asn
-
 Thermococcus kodakarensis
3.5.1.1 L-asparaginase
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.1 90
-
-
 Thermococcus kodakarensis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.1 70 100 the enzyme retains more than 50% activity between 70 and 100°C Thermococcus kodakarensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 90
-
 the enzyme retains almost 90% of its activity after 32 h incubation at 90°C Thermococcus kodakarensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.1 694
-
 L-asparagine at pH 8.0 and 90°C Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.1 8
-
-
 Thermococcus kodakarensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.1 6 10 the enzyme retains 20-90% of its activity between pH 6.0 and 10.0 Thermococcus kodakarensis