| Type: | Active_site | Name: | Alkaline phosphatase, active site |
| Description: | Alkaline phosphatase () (ALP) [] is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH. It is found in nearly all living organisms, with the exception of some plants. In Escherichia coli, ALP is found in the periplasmic space. In yeast, it is found in lysosome-like vacuoles and in mammals, it is aglycoprotein attached to the membrane by a GPI-anchor.In mammals, four different isozymes are currently known []. Three of them are tissue-specific: the placental, placental-like (germ cell) and intestinalisozymes. The fourth form is tissue non-specific and was previously known as the liver/bone/kidney isozyme.Streptomyces species involved in the synthesis of streptomycin (SM), an antibiotic, express a phosphatase () (gene strK) which is highly related to ALP. It specifically cleaves both streptomycin-6-phosphate and, more slowly, streptomycin-3"-phosphate []. This entry represents the ALP active site, and includes the region around the active site serine. It also matches the active site of the related enzyme, streptomycin-6-phosphate phosphatase. | Short Name: | Alkaline_phosphatase_AS |
