Literature summary for 4.3.1.1 extracted from

Giorgianni, F.; Beranova, S.; Wesdemiotis, C.; Viola, R.E.
Mapping the mechanism-based modification sites in L-aspartase from Escherichia coli (1997), Arch. Biochem. Biophys., 341, 329-336.

Search for more literature for 4.3.1.1

Inhibitors

Inhibitors	Comment	Organism	Structure
aspartate beta-semialdehyde	-	Escherichia coli
fumaric acid aldehyde	-	Escherichia coli
fumaric acid aldehyde ethyl ester	-	Escherichia coli
additional information	-	Escherichia coli
o-phospho-D-serine	competitive	Escherichia coli
O-phospho-L-serine	competitive	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.54	-	L-aspartate	C273A mutant, pH 7.0	Escherichia coli
0.6	-	L-aspartate	C140S/C273A mutant, pH 7.0	Escherichia coli
1.2	-	L-aspartate	wild-type, pH 7.0	Escherichia coli
1.3	-	L-aspartate	C273S mutant, pH 7.0	Escherichia coli
12	-	L-aspartate	K139I mutant, pH 7.0	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	C273S, C273A, C140S/C273A, K139I (mutants)	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate	r	Escherichia coli	fumarate + NH3	-	?
L-aspartate	absolutely specific	Escherichia coli	fumarate + NH3	-	?
L-aspartate	natural substrate	Escherichia coli	fumarate + NH3	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	-	Escherichia coli

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Release 2023.1 (January 2023)