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ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.

Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.

Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.

DCTPP1, also known as dCTP pyrophosphatase 1, contains an epilepsy-associated repeat (EAR) domain that is predicted to participate in protein-protein interactions, most likely involved in ligand recognition. This protein functions to hydrolyze abnormal nucleotide triphosphates (NTPs) in cancer cells that, if unregulated, could be incorporated into nascent DNA or RNA.

Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.

CTDSP1 is a class 2C phosphatase with activity dependent on the conserved DxD motif. CTDSP1 preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. In addition, CTDSP1 negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation.

Inositol Monophosphatase Domain Containing 1 or IMPAD1 is a protein, part of the inositol monophosphatase group of proteins. The protein is found in Golgi apparatus and enhances phosphoadenosine phosphate hydrolysis to adenosine monophosphate. When Mutation in the IMPAD1 gene occurs leads to GRAPP type chondrodysplasia and therefore joint dislocations. On long arm chromosome 1 a pseudogene can be found.

SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.

PPA1 is a member of the PPase family. PPA1 catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Many biochemical pathways use the hydrolysis of PPi to two phosphate ions to make the reactions permanently irreversible. A prominent illustration of this phenomenon is the inorganic pyrophosphatase catalyzation in the hydrolysis reaction at the beginning of lipid degradation. Inorganic pyrophosphatase provides the motivation for the activation of fatty acids destined for oxidation by stimulating the rapid hydrolysis of pyrophosphate.

Alkaline Phosphatase Liver/Bone/Kidney (Alpl) is a part of the alkaline phosphatases family which comprises 4 related alkaline phosphatases. Alpl is a membrane-bound glycosylated enzyme which is not expressed in any particular tissue. Alpl takes part in skeletal mineralization.

Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

7-methylguanosine phosphate-specific 5'-nucleotidase (NT5C3B) includes transferase activity and nucleotide binding. Among NT5C3B’s related super-pathways are adenosine nucleotides degradation II and Pyrimidine metabolism. NT5C3B hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP guards cells against undesired retrieval of m(7)GMP and its incorporation into nucleic acids. In addition, NT5C3B has weak activity for CMP.

Placental alkaline phosphatase (PLAP) is a membrane-associated siaglycoprotein enzyme normally present at high concentration in syncytiotrophoblasts within the placenta during the third trimester of gestation. The expression of PLAP was originally thought to be restricted to term placenta but a human PLAP-like variant has been described which shares more than 85% homology with PLAP itself. PLAP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It is also commonly expressed in germ cell tumors and more recently described in seminomas.

Fructose-1,6-bisphosphatase isozyme 2 (FBP2) is a part of the FBPase class 1 family. FBP2 is a gluconeogenesis regulatory enzyme Which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.

Ectonucleotide Pyrophosphatase-2, aka ENPP2, a part of the ectonucleotide pyrophosphatasefamily. ENPP2 is able to cut the phosphodiester bond between the alpha and the beta position of triphosphate nucleotides, acting as an ectonucleotide phosphodiesterase producing pyrophosphate, as most members of the ENPP family. It is unlike ENPP-1 and ENPP-3, has weak activity against nucleotides, but shows a lysophospholipase D activity which allows the formation of LPA and choline from lysophosphatidylcholine. As well, ENPP-2 and LPA are involved in several inflammatory-driven diseases such as arthritis and asthma.

PPA2 shares great imagination with members of the inorganic pyrophosphatase (PPase) family. PPA2 is localized to the mitochondrion and owns the signature sequence necessary for the catalytic activity of PPase. PPases catalyze the hydrolysis of pyrophosphate to inorganic phosphate, which is vital for the phosphate metabolism of cells.

PDXP is the active form of vitamin B6 that functions as a coenzyme in preserving biochemical homeostasis. The desired degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP. PDXP shows activity to pyridoxal 5''-phosphate (PLP), pyridoxine 5''-phosphate (PMP) and Pyridoxine 5''-phosphate (PNP), with a highest activity with PLP followed by PNP.

Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.

Ectonucleotide Pyrophosphatase (ENPP1) belongs to the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family. ENPP1 is a type II transmembrane glycoprotein comprised of 2 identical disulfide-bonded subunits. The ENPP1 protein has broad specificity and cleaves various substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. The ENPP1 protein can hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and it may also hydrolyze diadenosine polyphosphates. ENPP1 gene mutations are linked with 'idiopathic' infantile arterial calcification and ossification of the posterior longitudinal ligament of the spine (OPLL).

FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

Inositol monophosphatase1 (IMPA1) is responsible for the provision of inositol essential for synthesis of phosphatidylinositol and polyphosphoinositides. IMPA1 has a central role in the phosphatidylinositol signaling pathway by catalyzing the hydrolysis of inositol monophosphates. IMPA1 has been recognized as the pharmacological target for lithium action in the brain. The IMPA1 enzyme has a magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. Inhibition of inositol monophosphate hydroylosis and ensuing depletion of inositol for phosphatidylinositol synthesis may perhaps explain the anti-manic and anti-depressive effects of lithium administered to treat bipolar disorder.

ITPA enzyme catalyzes the pyrophosphohydrolysis of both ITP (inosine triphosphate) and dITP (deoxyinosine triphosphate) to IMP (inosine monophosphate) and diphosphate. IMP is exercised as a substrate for purine nucleotide pathways. IMP is phosphorylated to ITP, and ITPA mediates the concentration of ITP in the cell by changing ITP back to IMP. Defects in ITPA result in ITPA deficiency which is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.

FBP1 or Fructose-1, 6-bisphosphatase 1 is an enzyme, catalyzing the formation of fructose 6-phosphate & inorganic phosphate from fructose 1, 6-bisphosphate. FBP1 is part of the gluconeogenesis regulatory enzymes. Mutations in the enzyme gene can result in metabolic acidosis & hypoglycemia.