Published Online: 15 AUG 2014
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Liu, A. and Huo, L. 2014. Amidohydrolase Superfamily. eLS. .
- Published Online: 15 AUG 2014
The amidohydrolase superfamily is a structure-based cluster of enzymes that contain a sturdy and versatile triosephosphate isomerase (TIM)-like (β/α)8-barrel fold embracing the catalytic active site. To date, the amidohydrolase superfamily has grown into one of the largest families of enzymes, with tens of thousand of members catalysing a wide range of hydrolytic and nonhydrolytic metabolic reactions which are important in amino acid and nucleotide metabolism as well as biodegradation of agricultural and industrial compounds. Previously, the presence of a mono- or dinuclear d-block metal cofactor in the active site was thought to be one of the main characteristics of the members in this superfamily. However, recently new members containing a trinuclear metal cofactors or no cofactor at all were discovered. It has become apparent that activating a well-ordered water molecule by an active site residue for nucleophilic attack on the organic substrate is a common mechanistic feature for all members of the superfamily.
Amidohydrolase superfamily is one of the largest enzyme superfamilies performing a wide array of catalytic reactions.
All members in the family employ a TIM-barrel structural fold, although some of the amidohydrolase superfamily members present an imperfect barrel.
The vast majority, but not all, of the enzymes in this superfamily are metalloenzymes.
The hallmark of the catalytic mechanisms shared by these enzymes is to use an activated water molecule to attack the organic substrate.
The catalytic centre is diverse, with one, two, three or zero metal ion(s).
- metal cofactor;
- TIM-barrel structural fold;