Insights into acylphosphatase structure and catalytic mechanism
Rent the article at a discountRent now
* Final gross prices may vary according to local VAT.Get Access
Acylphosphatase is one of the smallest enzymes known (about 98 amino acid residues). It is present in organs and tissues of vertebrate species as two isoenzymes sharing over 55% of sequence homology; these appear highly conserved in differing species. The two isoenzymes can be involved in a number of physiological processes, though their effective biological function is not still certain. The solution and crystal structures of different isoenzymes are known, revealing a close packed protein with a fold similar to that shown by other phosphate-bind ing proteins. The structural data, together with an extended site-directed mutagenesis investigation, led to the identification of the residues involved in enzyme catalysis. However, it appears unlikely that these residues are able to perform the full catalytic cycle: a substrate-assisted catalytic mechanism has therefore been proposed, in which the phosphate moiety of the substrate could act as a nucleophile activating the catalytic water molecule.
- Insights into acylphosphatase structure and catalytic mechanism
Cellular and Molecular Life Sciences CMLS
Volume 53, Issue 2 , pp 141-151
- Cover Date
- Print ISSN
- Online ISSN
- Birkhäuser Verlag
- Additional Links
- Key words. Acylphosphatase isoenzymes; acylphosphatase, catalytic mechanism; acylphosphatase, catalytic residues; acylphosphatase, structure.
- Industry Sectors