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{PDOC00113}
{PS00123; ALKALINE_PHOSPHATASE}
{BEGIN}
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* Alkaline phosphatase active site *
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Alkaline phosphatase (EC 3.1.3.1) (ALP) [1] 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 (gene phoA) is found in the periplasmic space. In yeast
it (gene PHO8) is found in lysosome-like vacuoles and in mammals, it is a
glycoprotein attached to the membrane by a GPI-anchor.
In mammals, four different isozymes are currently known [2]. Three of them are
tissue-specific: the placental, placental-like (germ cell) and intestinal
isozymes. 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 (EC 3.1.3.39) (gene strK) which is highly
related to ALP. It specifically cleaves both streptomycin-6-phosphate and,
more slowly, streptomycin-3"-phosphate.
A serine is involved in the catalytic activity of ALP. The region around the
active site serine is relatively well conserved and can be used as a signature
pattern.
-Consensus pattern: [IV]-x-D-S-[GAS]-[GASC]-[GAST]-[GA]-T
[S is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 3.
-Last update: June 1994 / Text revised.
[ 1] Trowsdale J., Martin D., Bicknell D., Campbell I.
"Alkaline phosphatases."
Biochem. Soc. Trans. 18:178-180(1990).
PubMed=2379681
[ 2] Manes T., Glade K., Ziomek C.A., Millan J.L.
"Genomic structure and comparison of mouse tissue-specific alkaline
phosphatase genes."
Genomics 8:541-554(1990).
PubMed=2286375
[ 3] Mansouri K., Piepersberg W.
"Genetics of streptomycin production in Streptomyces griseus:
nucleotide sequence of five genes, strFGHIK, including a phosphatase
gene."
Mol. Gen. Genet. 228:459-469(1991).
PubMed=1654502
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{END}
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