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Literature summary extracted from

  • Li, J.; Wang, J.; Bachas, L.G.
    Biosensor for asparagine using a thermostable recombinant asparaginase from Archaeoglobus fulgidus (2002), Anal. Chem., 74, 3336-3341.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.1 analysis biosensor for asparagine using a thermostable recombinant asparaginase from Archaeoglobus fulgidus immobilized in front of an ammonium-selective electrode. The biosensor has a detection limit of 0.06 mM for L-asparagine. It shows high stability Archaeoglobus fulgidus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1 expression in Escherichia coli as a fusion protein with a polyhistidine tail Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 0.005
-
 L-asparagine pH 9.2, 70°C, recombinant enzyme Archaeoglobus fulgidus
3.5.1.1 0.08
-
 L-asparagine pH 9.2, 37°C, recombinant enzyme Archaeoglobus fulgidus
3.5.1.1 0.2
-
 L-glutamine pH 9.2, 70°C, recombinant enzyme Archaeoglobus fulgidus
3.5.1.1 0.35
-
 L-glutamine pH 9.2, 37°C, recombinant enzyme Archaeoglobus fulgidus
3.5.1.1 1.2
-
 D-asparagine pH 9.2, 70°C, recombinant enzyme Archaeoglobus fulgidus
3.5.1.1 1.8
-
 D-asparagine pH 9.2, 37°C, recombinant enzyme Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Archaeoglobus fulgidus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1 after heat treatment to denature most of the native Escherichia coli proteins, the enzyme is purified by an immobilized metal ion affinity chromatography method Archaeoglobus fulgidus

Storage Stability

EC Number Storage Stability Organism
3.5.1.1 22°C, pH 9.2, 4 months, the enzyme retains about 90% of enzyme activity Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 D-asparagine + H2O catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine Archaeoglobus fulgidus D-aspartate + NH3
-
 ?
3.5.1.1 L-asparagine + H2O catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine Archaeoglobus fulgidus L-aspartate + NH3
-
 ?
3.5.1.1 L-glutamine + H2O recombinant enzyme has 4fold higher activity for L-asparagine than for L-glutamine Archaeoglobus fulgidus L-glutamate + NH3
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 80
-
 5 min, stable Archaeoglobus fulgidus
3.5.1.1 85
-
 5 min, 30% loss of activity Archaeoglobus fulgidus
3.5.1.1 95
-
 5 min, 90% loss of activity Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.1 9.2
-
-
 Archaeoglobus fulgidus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.1 8 10 pH 8.0: about 70% of maximal activity, pH 10.0: about 85% of maximal activity Archaeoglobus fulgidus