| EC |
3.1.3.1 |
| Accepted name: |
alkaline phosphatase |
| Reaction: |
a phosphate monoester + H2O = an alcohol + phosphate |
| Other name(s): |
alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum) |
| Systematic name: |
phosphate-monoester phosphohydrolase (alkaline optimum) |
| Comments: |
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase) |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-78-9 |
| References: |
| 1. |
Engström, L. Studies on calf-intestinal alkaline phosphatase. I. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme. Biochim. Biophys. Acta 52 (1961) 36–48. [DOI] [PMID: 13890304] |
| 2. |
Harkness, D.R. Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme. Arch. Biochem. Biophys. 126 (1968) 513–523. [DOI] [PMID: 4970479] |
| 3. |
Malamy, M.H. and Horecker, B.L. Purification and crystallization of the alkaline phosphatase of Escherichia coli. Biochemistry 3 (1964) 1893–1897. [PMID: 14269306] |
| 4. |
Morton, R.K. Alkaline phosphatase of milk. 2. Purification of the enzyme. Biochem. J. 55 (1953) 795–800. [PMID: 13115375] |
| 5. |
Stadtman, T.C. Alkaline phosphatases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 55–71. |
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| [EC 3.1.3.1 created 1961] |
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