Literature summary for 3.5.1.1 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 .

Search for more literature for 3.5.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pectobacterium carotovorum

Organism

Organism	UniProt	Comment	Textmining
Pectobacterium carotovorum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
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]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
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)

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

Temperature Stability [°C]

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)