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PROSITE documentation PDOC00538 |
Acid phosphatases (EC 3.1.3.2) are a heterogeneous group of proteins that hydrolyze phosphate esters, optimally at low pH. It has been shown [1] that a number of acid phosphatases, from both prokaryotes and eukaryotes, share two regions of sequence similarity, each centered around a conserved histidine residue. These two histidines seem to be involved in the enzymes' catalytic mechanism [2,3]. The first histidine is located in the N-terminal section and forms a phosphohistidine intermediate while the second is located in the C-terminal section and possibly acts as proton donor. Enzymes belonging to this family are called 'histidine acid phosphatases' and are listed below:
April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | van Etten R.L. Davidson R. Stevis P.E. MacArthur H. Moore D.L. |
Source | J. Biol. Chem. 266:2313-2319(1991). |
2 | Authors | Ostanin K. Harms E.H. Stevis P.E. Kuciel R. Zhou M.-M. Van Etten R.L. |
Title | Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. | |
Source | J. Biol. Chem. 267:22830-22836(1992). | |
PubMed ID | 1429631 |
3 | Authors | Schneider G. Lindqvist Y. Vihko P. |
Title | Three-dimensional structure of rat acid phosphatase. | |
Source | EMBO J. 12:2609-2615(1993). | |
PubMed ID | 8334986 |