Search results
Results From The WOW.Com Content Network
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 ]
Some common regulatory subunits include GM (PPP1R3A) and GL (PPP1R3B), which are named after their locations of action within the body (muscle and liver respectively), [5] While the yeast S. cerevisiae only encodes one catalytic subunit, mammals have four isozymes encoded by three genes, each attracting a different set of regulatory subunits. [4]
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]
, is the only species present. At pH 13 or higher, the acid is completely dissociated as the phosphate ion, (PO 4) 3−. This means that salts of the mono- and di-phosphate ions can be selectively crystallised from aqueous solution by setting the pH value to either 4.7 or 9.8. In effect, H 3 PO 4, H 2 (PO 4) − and H(PO 4) 2−
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]
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 ...
A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (), with up to 30% of all proteins being phosphorylated at any given time.
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 .