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Literature summary extracted from

  • Faret, M.; de Morais, S.B.; Zanchin, N.I.T.; de Souza, T.A.C.B.
    L-Asparaginase from Erwinia carotovora insights about its stability and activity (2019), Mol. Biol. Rep., 46, 1313-1316 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1 expression in Escherichia coli Pectobacterium carotovorum

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Pectobacterium carotovorum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1 recombinant enzyme, changes in the solubilization conditions of the L-asparaginase may increase by up to 25% its enzymatic activity Pectobacterium carotovorum

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 additional information
-
L-asparaginase activity depends on buffers and ions and ranges from 386 I.U/mg in 50 mM sodium phosphate buffer pH 6.0, 375 mM NaCl up to 510 I.U/mg in 50 mM Tris-HCl pH 7.5, 500 mM NaCl Pectobacterium carotovorum

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 34
-
melting temperature, 50 mM sodium phosphate buffer, pH 6.0, 375 mM NaCl Pectobacterium carotovorum
3.5.1.1 39
-
melting temperature, 50 mM MES pH 6.0 Pectobacterium carotovorum
3.5.1.1 41.5
-
melting temperature, 50 mM Tris-HCl pH 9.0 Pectobacterium carotovorum