Literature summary for 2.6.1.17 extracted from

Graindorge, M.; Giustini, C.; Kraut, A.; Moyet, L.; Curien, G.; Matringe, M.
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms (2014), J. Biol. Chem., 289, 3198-3208.

Search for more literature for 2.6.1.17

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.021	-	prephenate	pH 8.0, 30°C	Streptomyces avermitilis

Organism

Organism	UniProt	Comment	Textmining
Streptomyces avermitilis	Q82IK5	bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79	-
Streptomyces avermitilis DSM 46492	Q82IK5	bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
prephenate + N-succinyl-L-2,6-diaminoheptanedioate	-	Streptomyces avermitilis	L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate	-	?
prephenate + N-succinyl-L-2,6-diaminoheptanedioate	-	Streptomyces avermitilis DSM 46492	L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate	-	?

Synonyms

Synonyms	Comment	Organism
AspB2	-	Streptomyces avermitilis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
24	-	prephenate	pH 8.0, 30°C	Streptomyces avermitilis

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)