Literature summary for 3.1.1.6 extracted from

DAmbrosio, C.; Mandrich, L.; Rossi, M.; Scaloni, A.; Manco, G.
A proteomic approach to study Escherichia coli. Acetyl esterase interactors unveil a sequence motif involved in protein-protein interaction (2008), Protein Pept. Lett., 15, 333-340.

Search for more literature for 3.1.1.6

Application

Application	Comment	Organism
molecular biology	protein-protein interaction consensus sequence, involved in regulation of both sugar and lipid metabolism, according to interaction partners	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
structural superimposition of homology-generated model with Alicyclobacillus acidocaldarius EST2 and Escherichia coli beta-cystathionase MalY revealed nine amino acid consensus sequence putatively involved in protein-protein interactions, amino acids 178-184 are putative core of interaction with MalY and MalT	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
R179A	mutation in interaction consensus sequence, wild-type activity, loss of interaction with Aes interactors such as MalY	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
from bacterial extracts by binding to CNBr-activated Sepharose CL6B, 1.5 mg bound protein per ml resin, pH 8.3, 0.1 M sodium hydrogen carbonate, 0.5 M sodium chloride	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	activated Sepharose CL6B-bound activity, pH 8	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
dimer	determined by affinity using pull down	Escherichia coli

Synonyms

Synonyms	Comment	Organism
Acetyl esterase	-	Escherichia coli
Aes	-	Escherichia coli

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Release 2023.1 (January 2023)