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Phenylalanine hydroxylase

Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyses the reaction responsible for the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine.

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Phosphodiesterases

Phosphodiesterase is any enzyme that breaks a phosphodiester bond. Phosphodiesterase enzymes are often targets for pharmacological inhibition due to their unique tissue distribution, structural properties, and functional properties. However, there are many other families of phosphodiesterases, including phospholipases C and D, autotaxin, sphingomyelin phosphodiesterase, DNases, RNases, and restriction endonucleases, as well as numerous less-well-characterized small-molecule phosphodiesterases.

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Phosphoenolpyruvate carboxykinase

Phosphoenolpyruvate carboxykinase (PEPCK) is an enzyme in the lyase family used in the metabolic pathway of gluconeogenesis. It converts oxaloacetate into phosphoenolpyruvate and carbon dioxide.

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Phosphoenolpyruvate carboxylase

Phosphoenolpyruvate carboxylase ( EC 4.1.1.31) is an enzyme in the family of carboxy-lyases that catalyzes the addition of bicarbonate to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate.

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Phosphoglucomutase

Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on a glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. It facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate.

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Phosphogluconate 2-dehydrogenase

Phosphogluconate 2-dehydrogenase (EC 1.1.1.43) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase.This enzyme participates in pentose phosphate pathway and glutathione metabolism.

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Phosphoglycerate dehydrogenase

D-3-phosphoglycerate dehydrogenase is an enzyme that catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first and rate-limiting step in the phosphorylated pathway of serine biosynthesis, using NAD+/NADH as a cofactor.

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Phospholipase A2

Phospholipases A2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophosphatidic acid.Phospholipases A2 enzymes are commonly found in mammalian tissues as well as arachnid, insect and snake venom.Phospholipases A2 include several unrelated protein families with common enzymatic activity. Two most notable families are secreted and cytosolic phospholipases A2. Other families include Ca2+ independent PLA2 (iPLA2) and lipoprotein-associated PLA2s (lp-PLA2), also known as platelet activating factor acetylhydrolase (PAF-AH).Pancreatic sPLA2 serve for the initial digestion of phospholipid compounds in dietary fat.

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Phospholipase C

Phospholipase C (PLC) is a class of enzymes that cleave phospholipids just before the phosphate group . It is most commonly taken to be synonymous with the human forms of this enzyme, which plays an important role in eukaryotic cell physiology, in particular signal transduction pathways. Thirteen kinds of mammalian phospholipase C are classified into six models (β, γ, δ, ε, ζ, η) according to structure.

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Phosphonoacetaldehyde

Phosphonoacetaldehyde is a substrate of the enzyme Phosphonoacetaldehyde hydrolase that catalyzes the chemical reaction.

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