Literature summary for 4.3.1.1 extracted from

Kong, X.; Li, Z.; Gou, X.; Zhu, S.; Zhang, H.; Wang, X.; Zhang, J.
A monomeric L-aspartase obtained by in vitro selection (2002), J. Biol. Chem., 277, 24289-24293.

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Protein Variants

Protein Variants	Comment	Organism
additional information	design of enzyme variants by ligation of subdomains with a random hexapeptide loop, variant with highest activity is a monomer with high thermotolerance	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
50	-	30 min, 17% residual activity, wild type enzyme	Escherichia coli
50	-	30 min, 80% residual activity, monomeric enzyme variant	Escherichia coli

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Release 2023.1 (January 2023)