Member database | PRINTS |
PRINTS type | domain |
Short name | ABHYDROLASE |
Description Imported from IPR000073
This entry represents fold-1 of α/β hydrolases.
The α/β hydrolase fold
[1] is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an α/β-sheet (rather than a barrel), containing 8 strands connected by helices
[1]. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best conserved structural features of the fold. Esterase (EST) from Pseudomonas putida is a member of the α/β hydrolase fold superfamily of enzymes
[2].
In most of the family members the β-strands are parallel, but some have an inversion of the first strands, which gives it an antiparallel orientation. The catalytic triad residues are presented on loops. One of these is the nucleophile elbow and is the most conserved feature of the fold. Some other members lack one or all of the catalytic residues. Some members are therefore inactive but others are involved in surface recognition. The ESTHER database
[3] gathers and annotates all the published information related to gene and protein sequences of this superfamily
[3].
References Imported from IPR000073
1.The alpha/beta hydrolase fold. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J. Protein Eng. 5, 197-211, (1992). View articlePMID: 1409539
2.Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis. Elmi F, Lee HT, Huang JY, Hsieh YC, Wang YL, Chen YJ, Shaw SY, Chen CJ. J. Bacteriol. 187, 8470-6, (2005). View articlePMID: 16321951
3.ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins. Hotelier T, Renault L, Cousin X, Negre V, Marchot P, Chatonnet A. Nucleic Acids Res. 32, D145-7, (2004). View articlePMID: 14681380