Literature summary for 4.3.1.1 extracted from

Novikov, A.; Derbikov, D.; Shaposhnikova, O.; Gubanova, T.; Kameneva, S.; Yanenko, A.
The highly efficient expression of the aspartase gene (L-aspartate ammonia-lyase) in Escherichia coli cells (2015), Appl. Biochem. Microbiol., 51, 751-756 .

No PubMed abstract available

Search for more literature for 4.3.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
cloning in the pLATE31 plasmid composition and highly efficient expression under the control of the T7 phage promoter in Escherichia coli BLR (DE3) cell. The use of the expression system allows an increase in aspartase activity in cells by 100times as compared to the initial strain. The maximal specific activity of cells reached 0.700 mM/mg/min	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
52000	-	SDS-PAGE	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli VKPM V-7188	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
700	-	activity in Escherichia coli BLR (DE3) cells after cloning the enzyme in the pLATE31 plasmid, composition and highly efficient expression under the control of the T7 phage promoter, pH and temperature not specified in the publication	Escherichia coli

Subunits

Subunits	Comment	Organism
?	x * 52000, SDS-PAGE	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ASPA	-	Escherichia coli
aspartase	-	Escherichia coli
L-aspartate ammonia-lyase	-	Escherichia coli

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Release 2023.1 (January 2023)