Literature summary for 2.6.1.1 extracted from

Liu, D.; Pozharski, E.; Fu, M.; Silverman, R.B.; Ringe, D.
Mechanism of inactivation of Escherichia coli aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (2010), Biochemistry, 49, 10507-10515.

Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
two nearly identical crystal structures of the complexes between (S)-4-amino-4,5-dihydro-2-furancarboxylic acid and L-AspAT obtained at pH 7.5 and 8 are shown. The inhibitor forms only one adduct with the enzyme, with active site lysine 246, thus irreversibly inactivating the L-AspAT transamination reaction	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
(S)-4-amino-4,5-dihydro-2-furancarboxylic acid	crystal structures of the Escherichi coli aspartate aminotransferase with (S)-4-amino-4,5-dihydro-2-furancarboxylic acid bound to the active site are obtained via cocrystallization at pH 7.5 and 8. The complex structures suggest that (S)-4-amino-4,5-dihydro-2-furancarboxylic acid inhibits the transamination reaction by forming adducts with the catalytic lysine 246 via a covalent bond while producing 1 equivalent of pyridoxamine 5'-phosphate	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	D3H0F7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate + 2-oxoglutarate	-	Escherichia coli	oxaloacetate + L-glutamate	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
L-AspAT	-	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Escherichia coli

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)