Download MendeleyCrystal structure of common type acylphosphatase from bovine testis.
Thunnissen, M.M., Taddei, N., Liguri, G., Ramponi, G., Nordlund, P.(1997) Structure 5: 69-79
- PubMed: 9016712
- DOI: https://doi.org/10.1016/s0969-2126(97)00167-6
- Primary Citation of Related Structures:
2ACY - PubMed Abstract:
Acylphosphatase (ACP) is a low molecular weight phosphomonohydrolase catalyzing with high specificity the hydrolysis of the carboxyl-phosphate bond present in acylphosphates. The enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and the production of ribonucleotides. Furthermore the enzyme is capable of hydrolyzing the phospho-aspartyl intermediate formed during the action of membrane pumps such as (Ca2++Mg2+) ATPase. Although the tertiary structure of a muscle ACP has been determined by NMR spectroscopy, little is known about the catalytic mechanism of ACP and further structures might provide an increased understanding.
Organizational Affiliation:
Department of Molecular Biology, University of Stockholm, S-106 91, Stockholm, Sweden.
