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Glycogen phosphorylase is one of the phosphorylaseenzymes(EC2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase.
Glycogen phosphorylase can only act on linearchainsof glycogen(a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch(which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidaseenzymeis required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue.
An insulinstimulated enzyme known as phosphoprotein phosphatase(PP-1) inactivates glycogen phosphorylase to prevent glycogen break up.
GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting.

Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.

UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

Uridine phosphorylase from Salmonella typhimurium (StUP) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.

Thymidine phosphorylase precursor (TYMP) is a platelet-derived endothelial cell growth factor that catalyzes the formation of thymine and 2-deoxy-D-ribose-1-phosphate from thymidine and orthophosphate. TYMP is an angiogenic inducer that potently stimulates the growth of endothelial cells and induces chemotaxis. TYMP has a highly restricted target cell specificity acting only on endothelial cells. An increased expression of TYMP is found in a broad array of different solid tumors and inflammatory diseases and is frequently associated with poor prognosis. Mutations in the TYMP gene are linked to mitochondrial neurogastrointestinal encephalomyopathy.

PNP is a member of the PNP/MTAP phosphorylase family of proteins. PNP catalyzes the reversible phosphorolysis of ribonucleosides and 2’-deoxyribonucleosides with specificity for guanine, hypoxanthine and their analogs. PNP deficiency is a rare autosomal recessive genetic disease linked to a severe defect in T-lymphocyte function and neurologic disorder in children, comprising four percent of combined immunodeficiency cases.

UDP-Glucose Pyrophosphorylase 2, also known as UGP2 is an essential intermediary in mammalian carbohydrate inter conversions. UGP2 transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. UDP-glucose is a direct precursor of glycogen in the liver and muscle tissue, moreover in lactating mammary gland it is converted to UDP-galactose which is next converted to lactose.

Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
and Fermentation.  Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways.

PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

Pyridoxal phosphate phosphatase PHOSPHO2, orphan 2 (PHOSPHO2) is a member of the haloacid dehalogenase (HAD) superfamily. Phosphatase has an elevated activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). PHOSPHO 1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralizing cells and is believed to be implicated in the production of inorganic phosphate for bone mineralization. PHOSPHO2 is a recognized phosphatase sharing a 42% sequence identity with PHOSPHO1. PHOSPHO1 and PHOSPHO2 are especially similar, however surprisingly recombinant PHOSPHO2 hydrolyses phosphoethanolamine and phosphocholine comparatively inadequately.

Phosphoribosylaminoimidazole Carboxylase (PAICS) is an enzyme involved in nucleotide biosynthesis and particularly in purine biosynthesis. PAICS is a bifunctional enzyme containing phosphoribosylaminoimidazole carboxylase activity at its N-terminal region and phosphoribosylaminoimidazole succinocarboxamide synthetase at its C-terminal region. PAICS catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole(AIR) into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole (CAIR) as described in the reaction. PAICS catalyzes steps six and seven of purine biosynthesis.

APRT is part of the purine/pyrimidine phosphoribosyltransferase family. APRT enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). APRT produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in APRT causes 2,8-dihydroxyadenine urolithiasis. APRT catalyzes a salvage reaction resulting in the formation of AMP.

AK4 belongs to the adenylate kinase family of enzymes. AK4 protein is restricted to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide structures in a cell by catalyzing the reversible transfer of phosphate group among these nucleotides. Hereditary mutations which cause AK4 deficiencies in erythrocytes have been associated to hemolytic anemia.

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.

Prostatic acid phosphatase, also known as PAP, is an enzyme produced by the prostate. PAP may be found in increased amounts in men with prostate cancer.
PAP’s physiological function may be associated with the liquefaction process of semen.
The highest levels of PAP are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells (sickle-cell disease) or multiple myeloma or lysosomal storage diseases (Gaucher's disease), will show moderately higher levels.
Certain medications can cause temporary changes in PAP levels. Manipulation of the prostate gland through rectal exam, biopsy or massage may increase the level.

Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.

PGLS is an enzyme in the second step pentose phosphate pathway. 6-Phosphogluconolactonase is crucial for the synthesis of nucleotide sugars and NADPH, the key cause for decreasing power. PGLS transforms 6-phosphogluconolactone to 6-phosphogluconate.

Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.

PCYT2 is a member of the cytidylyltransferase family. PCYT2 is an enzyme which catalyzes the formation of CDP-MEA from CTP and phospho MEA in the Kennedy pathway of phospholipid synthesis. PCYT2 has the strongest expression in the liver, heart, and skeletal muscle.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.