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Literature summary extracted from

  • Kotzia, G.A.; Labrou, N.E.
    L-Asparaginase from Erwinia chrysanthemi 3937: cloning, expression and characterization (2006), J. Biotechnol., 127, 657-669.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.1 medicine the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C. The approach offers the possibility of designing an L-asparaginase from Erwinia chrysanthemi bioreactor that can be operated over a long period of time with high efficiency, which can be used in leukaemia therapy Dickeya chrysanthemi

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1 expression in Escherichia coli BL21(DE3)pLysS Dickeya chrysanthemi
3.5.1.1 expression in Escherichia coli strain BL21(DE3) Dickeya chrysanthemi

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 additional information immobilization of the purified recombinant enzyme on epoxy-activated resin, the immobilized enzyme retains 60% of maximal activity and is highly stable at 4°C, utilization as bioreactor Dickeya chrysanthemi

General Stability

EC Number General Stability Organism
3.5.1.1 the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C Dickeya chrysanthemi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 additional information
-
 additional information kinetics Dickeya chrysanthemi
3.5.1.1 0.058
-
 L-asparagine pH 8, 37°C Dickeya chrysanthemi
3.5.1.1 0.8
-
 Nalpha-acetyl-Asn pH 8, 37°C Dickeya chrysanthemi
3.5.1.1 6.7
-
 L-Gln pH 8.2, 37°C Dickeya chrysanthemi
3.5.1.1 18.8
-
 succinamic acid pH 8, 37°C Dickeya chrysanthemi

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 Dickeya chrysanthemi
-
 L-aspartate + NH3
-
 ?
3.5.1.1 L-asparagine + H2O Dickeya chrysanthemi 3937
-
 L-aspartate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Dickeya chrysanthemi
-
-
-
3.5.1.1 Dickeya chrysanthemi Q6Q4F3
-
-
3.5.1.1 Dickeya chrysanthemi 3937
-
-
-
3.5.1.1 Dickeya chrysanthemi 3937 Q6Q4F3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1
-
 Dickeya chrysanthemi
3.5.1.1 recombinant enzyme from Escherichia coli strain BL21(DE3) in a single step procedure to homogeneity by cation exchange Dickeya chrysanthemi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O
-
 Dickeya chrysanthemi L-aspartate + NH3
-
 ?
3.5.1.1 L-asparagine + H2O
-
 Dickeya chrysanthemi 3937 L-aspartate + NH3
-
 ?
3.5.1.1 L-Gln + H2O
-
 Dickeya chrysanthemi L-Glu + NH3
-
 ?
3.5.1.1 L-Gln + H2O
-
 Dickeya chrysanthemi 3937 L-Glu + NH3
-
 ?
3.5.1.1 Nalpha-acetyl-L-Asn + H2O
-
 Dickeya chrysanthemi Nalpha-acetyl-L-Asp + NH3
-
 ?
3.5.1.1 Nalpha-acetyl-L-Asn + H2O
-
 Dickeya chrysanthemi 3937 Nalpha-acetyl-L-Asp + NH3
-
 ?
3.5.1.1 succinamic acid + H2O
-
 Dickeya chrysanthemi succinate + NH3
-
 ?
3.5.1.1 succinamic acid + H2O
-
 Dickeya chrysanthemi 3937 succinate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 ASNase
-
 Dickeya chrysanthemi
3.5.1.1 L-ASNase
-
 Dickeya chrysanthemi
3.5.1.1 L-asparaginase
-
 Dickeya chrysanthemi

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 37
-
 particularly stable at Dickeya chrysanthemi
3.5.1.1 46
-
 enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively Dickeya chrysanthemi
3.5.1.1 47
-
 enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively Dickeya chrysanthemi
3.5.1.1 57
-
 enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively Dickeya chrysanthemi
3.5.1.1 63
-
 enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively Dickeya chrysanthemi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.1 0.0043
-
 L-Gln pH 8.2, 37°C Dickeya chrysanthemi
3.5.1.1 0.0108
-
 Nalpha-acetyl-Asn pH 8, 37°C Dickeya chrysanthemi
3.5.1.1 0.0128
-
 L-asparagine pH 8, 37°C Dickeya chrysanthemi
3.5.1.1 0.0239
-
 succinamic acid pH 8, 37°C Dickeya chrysanthemi

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.1.1 Dickeya chrysanthemi pI calculated from sequence is 8.57
-
 8.6