Amidohydrolase Superfamily

Liu Aimin, University of Mississippi Medical Center, Jackson, Mississippi, USA
Li Tingfeng, University of Mississippi Medical Center, Jackson, Mississippi, USA
Fu Rong, University of Mississippi Medical Center, Jackson, Mississippi, USA

Published online: September 2007

DOI: 10.1002/9780470015902.a0020546

The amidohydrolase superfamily is a structure-based cluster of enzymes that contain a sturdy and versatile triosephosphate isomerase (TIM)-like -barrel embracing a mono- or dinuclear d-block metal cofactor essential for catalysis. Up to date, it has had several thousand members catalysing a wide range of hydrolytic and nonhydrolytic metabolic reactions important in amino acid and nucleotide metabolism as well as biodegradation of agricultural and industrial compounds.

Keywords: amidohydrolase; metal cofactor; TIM-barrel structural fold; enzymology; evolution

Figure 1. Metal cofactor and the TIM-like parallel barrel core in adenosine deaminase (ADA, from PDB file 1a4m). The metal ion is depicted as CPK sphere, Metal ligands are shown in sticks and the propeller structural fold is highlighted in blue colour in the representation. Substrate analogue 6-hydroxy-1,6-dihydro purine nucleoside is represented in scaled ball and stick. The fifth helix covering the segment of residues 223–228 is represented transparent for uncovering the strands. The ADA is a homotetramer in the structure; only the subunit A is shown.
Figure 2. An imperfect TIM-barrel exhibited in the structure of adenosine 5¢-monophosphate deaminase (AMPD) in complex with coformycin 5¢-phosphate (ball and stick) (from PDB file 2a3 l). The inset highlights the distorted barrel and the zinc ion (CPK sphere).
Scheme 1. Hydrolytic (a) and nonhydrolytic (b) reactions catalysed by the structurally characterized members of the amidohydrolase superfamily.
Scheme 2. Chemical reaction catalysed by 4-oxalomesaconate hydratase (OMAH).
Scheme 3. Adenosine deaminase catalytic cycle.
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Related Sub-Topics:

Protein Structure | Proteins: Structure, Function, Metabolism | Enzymes: Structure and Action Mechanism
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Article Title: Amidohydrolase Superfamily
 
How to Cite close
Aimin, Liu, Tingfeng, Li, and Rong, Fu(Sep 2007) Amidohydrolase Superfamily. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0020546]