Literature summary for 1.3.1.28 extracted from

Khalil, S.; Pawelek, P.D.
Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-protein interaction between Escherichia coli 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase (EntE) (2011), Biochemistry, 50, 533-545.

Search for more literature for 1.3.1.28

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
More	enzyme can form a specific complex with 2,3-dihydroxybenzoate-AMP ligase EntE. Cross-linked product with a molecular mass of more than 250 kDa, suggesting a complex stoichiometry of one EntA tetramer and four EntE monomers. Addition of a 4-fold excess of EntA to an EntE assay mixture results in a 6fold stimulation of EntE activity	Escherichia coli
More	enzyme undergoes concentration-dependent dimer-tetramer self-association with a KD value of 12.3 microM, analytical ultracentrifugation	Escherichia coli

Synonyms

Synonyms	Comment	Organism
EntA	-	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)