1. Home
  2. Family
  3. Acetyl_esterase

Acetyl_esterase

Relationship

Family: Acetyl_esterase

Block: H

Parent Family: No family

Comment

Extracted from Hormone sensitive lipases. Proteins in this entry belong to the 'GDXG' family of lypolytic enzymes and are also known as Aes proteins. They have esterase activity against short chain (up to 8 carbon atoms) fatty esters and are able to hydrolyse triacetin and tributyrin but not triolein or cholesterol oleate. These proteins are involved in the downregulation of the transcriptional activator of the maltose regulon, MalT, in E. coli. The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. HAMAP: MF_01958

Database

Interpro : IPR023508 Acetyl esterase

PIRSF : No PIRSF

Pdoc : No Pdoc

Pfam : No Pfam

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

References (3)

Title : Structural and mutational analyses of Aes, an inhibitor of MalT in Escherichia coli - Schiefner_2014_Proteins_82_268
Author(s) : Schiefner A , Gerber K , Brosig A , Boos W
Ref : Proteins , 82 :268 , 2014
Abstract : Schiefner_2014_Proteins_82_268
ESTHER : Schiefner_2014_Proteins_82_268
PubMedSearch : Schiefner_2014_Proteins_82_268
PubMedID: 23934774
Gene_locus related to this paper: ecoli-Aes

Title : The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism - Mandrich_2002_J.Biol.Chem_277_48241
Author(s) : Mandrich L , Caputo E , Martin BM , Rossi M , Manco G
Ref : Journal of Biological Chemistry , 277 :48241 , 2002
Abstract : Mandrich_2002_J.Biol.Chem_277_48241
ESTHER : Mandrich_2002_J.Biol.Chem_277_48241
PubMedSearch : Mandrich_2002_J.Biol.Chem_277_48241
PubMedID: 12374803
Gene_locus related to this paper: ecoli-Aes

Title : The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon - Joly_2002_J.Biol.Chem_277_16606
Author(s) : Joly N , Danot O , Schlegel A , Boos W , Richet E
Ref : Journal of Biological Chemistry , 277 :16606 , 2002
Abstract : Joly_2002_J.Biol.Chem_277_16606
ESTHER : Joly_2002_J.Biol.Chem_277_16606
PubMedSearch : Joly_2002_J.Biol.Chem_277_16606
PubMedID: 11867639
Gene_locus related to this paper: ecoli-Aes

Structures (3)

Genes Proteins in Acetyl_esterase family (61)

No fragment of genes

Structures in Acetyl_esterase family (3)

No substrate

Inhibitors in Acetyl_esterase family (3)