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A ball and stick model of a phosphate anion. In biochemistry, a phosphatase is an enzyme that uses water to cleave a phosphoric acid monoester into a phosphate ion and an alcohol. Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. [1]
Regulation of inorganic phosphate within the cellular system. The Phosphate (Pho) regulon is a regulatory mechanism used for the conservation and management of inorganic phosphate within the cell. It was first discovered in Escherichia coli as an operating system for the bacterial strain, and was later identified in other species. [1]
In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]
Phosphorus comprises 0.1% by mass of the average rock [12] (while, for perspective, its typical concentration in vegetation is 0.03% to 0.2%), [13] and consequently there are quadrillions of tons of phosphorus in Earth's 3×10 19-ton crust, [14] albeit at predominantly lower concentration than the deposits counted as reserves, which are ...
A key regulator of PP1 is glycogen phosphorylase a, which serves as a glucose sensor in hepatocytes. [12] When glucose levels are low, phosphorylase a in its active R state has PP1 bound tightly. This binding to phosphorylase a prevents any phosphatase activity of PP1 and maintains the glycogen phosphorylase in its active phosphorylated ...
In biochemistry, dephosphorylation is the removal of a phosphate (PO 3− 4) group from an organic compound by hydrolysis. It is a reversible post-translational modification . Dephosphorylation and its counterpart, phosphorylation , activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides .
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its ...
The glycerol phosphate shuttle was first characterized as a major route of mitochondrial hydride transport in the flight muscles of blow flies. [5] [6] It was initially believed that the system would be inactive in mammals due to the predominance of lactate dehydrogenase activity over glycerol-3-phosphate dehydrogenase 1 (GPD1) [5] [7] until high GPD1 and GPD2 activity were demonstrated in ...