2ACY

ACYL-PHOSPHATASE (COMMON TYPE) FROM BOVINE TESTIS

Summary for 2ACY

• Entry DOI: 10.2210/pdb2acy/pdb
• Descriptor: ACYLPHOSPHATASE, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: acylphosphatase, phosphoric monoester hydrolase
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 11326.11

Authors

Thunnissen, M.M.G.M.,Nordlund, P. (deposition date: 1996-11-08, release date: 1997-11-12, Last modification date: 2024-02-14)

Primary citation

Thunnissen, M.M.,Taddei, N.,Liguri, G.,Ramponi, G.,Nordlund, P.
Crystal structure of common type acylphosphatase from bovine testis.
Structure, 5:69-79, 1997

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.

PubMed: 9016712
DOI: 10.1016/S0969-2126(97)00167-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)