Physiological Functions of ALP

The bone isoenzyme has long been thought to have a role in normal skeletal
mineralization. The natural substrates for TNSALP appear to include at least three
phosphor compounds: phosphoethanolamine (PEA), inorganic pyrophosphate (PPi),
and pyridoxal-5′-phosphate (PLP), as evidenced by increased plasma and/or urinary
levels of each in subjects with hypophosphatasia, but this is uncertain. Indeed, a variety
of mechanisms have been proposed to explain the role of ALP in bone mineralization.
However, apart from its role in normal bone mineralization, the other functions of L/B/K
remains obscure both in physiological and neoplastic conditions.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4062654/
Physiology
In humans, alkaline phosphatase is present in all tissues throughout the body, but is
particularly concentrated in the liver, bile duct, kidney, bone, intestinal
mucosa and placenta. In the serum, two types of alkaline
phosphatase isozymes predominate: skeletal and liver. During childhood the majority of
alkaline phosphatase are of skeletal origin. Humans and most other mammals contain
the following alkaline phosphatase isozymes:

 ALPI – intestinal (molecular weight of 150 kDa)

 ALPL – tissue-nonspecific (expressed mainly in liver, bone, and kidney)
 ALPP – placental (Regan isozyme)
 ALPG – germ cell
Four genes encode the four isozymes. The gene for tissue-nonspecific alkaline
phosphatase is located on chromosome 1, and the genes for the other three isoforms
are located on chromosome. 
https://en.wikipedia.org/wiki/Alkaline_phosphatase

Structure and properties

Alkaline phosphatase is homodimeric enzyme, meaning it is formed with two molecules.
Three metal ions, two Zn and one Mg, are contained in the catalytic sites, and both
types are crucial for enzymatic activity to occur. The enzymes catalyze the hydrolysis of
monoesters in phosphoric acid which can additionally catalyze a transphosphorylation
reaction with large concentrations of phosphate acceptors. While the main features of
the catalytic mechanism and activity are conserved between mammalian and bacterial
alkaline phosphate, mammalian alkaline phosphatase has a higher specific activity
and Km values thus a lower affinity, more alkaline pH optimum, lower heat stability, and
are typically membrane bound and are inhibited by l-amino acids and peptides via a
means of uncompetitive mechanism. These properties noticeably differ between
different mammalian alkaline phosphatase isozymes and therefore showcase a
difference in in vivo functions.
Alkaline phosphatase has homology in a large number of other enzymes and composes
part of a superfamily of enzymes with several overlapping catalytic aspects and
substrate traits. This explains why most salient structural features of mammalian
alkaline are the way they are and reference their substrate specificity and homology to
other members of the nucleoside pyrophosphatase/phosphodiesterase family of
isozyme.[4] Research has shown a relationship between members of the alkaline
phosphatase family with aryl sulfatases. The similarities in structure indicate that these
two enzyme families came from a common ancestor. Further analysis has linked
alkaline phosphates and aryl sulfatases to a larger superfamily. Some of the common
genes found in this superfamily, are ones that encode phosphodiesterases as well as
autotoxin.

https://en.wikipedia.org/wiki/Alkaline_phosphatase