The function of Anti-PP2Ac

Anti-PP2Ac usually refers to the hydrolysis catalytic enzymes are collectively phosphate compound, or the hydrolysis of poly-phosphate, phosphoric acerbic admixture enzymes in general. Sometimes aswell referred to as polyphosphoric acerbic phosphatase enzymes and enzymes. The above mainly includes Phosphomonoesterase phosphodiesterase blazon and class. The closing has adenosine triphosphatase, pyrophosphatase, fractional phosphatase. Phosphatase is a way to accord to the phosphorylation of the substrate of the enzyme, i.e. by hydrolyzing the substrate phosphate monoester phosphate accumulation on the atom removed and generates phosphate ions and chargeless hydroxyl groups. The role of phosphatases and kinases contrary, phosphorylase kinase, can use the activity molecule, such as ATP, phosphate groups to accord to the substrate molecule. Are accepted in abounding bacilli is an acrid phosphatase. Phosphatases can be disconnected into two categories: cysteine-dependent phosphatase phosphatase and metals (in its activity depends on the alive website of the metal ion). First, the agitator alive website cysteine ​​on the abandon of nucleophilic groups advancing the phosphate accumulation of the phosphorus atom and bonding; Then, affix the phosphate accumulation and Tyrosine PO key to acquire the position of a acceptable acerb amino acids ( such as aspartic acid) or baptize molecules to accommodate protons protonated, thereby basic phosphoric acerbic - cysteine ​​intermediate; this average was anatomize added baptize molecules, the alive website of the agitator is appear and Proceed to the next dephosphorylation. Metal phosphatase alive website of a aggregate of two catalytic metal ions necessary. As for the attributes of these two metal ions allegation are not consistent, so far not yet conclusive.

Anti-PP2Ac with phosphorylase kinase or phosphorylation of the opposite. Phosphorylation can accomplish an agitator to be activated or deactivated, it can accomplish a protein - protein interactions (such as an SH3 domain); accordingly phosphatase abounding arresting transduction pathways appropriate for ascendancy of phosphorylation. It is account advertence that, phosphorylation or dephosphorylation do not necessarily accord to the activation or inhibition of the enzyme, and some enzymes accept assorted phosphorylation sites complex in the activation or inhibition of the regulation. For example, cyclin-dependent kinase (CDK) to be added than one specific phosphorylated amino acerbic residues, and the agnate activation or inhibition of phosphorylation of altered residues. The acumen phosphate signaling is important for the acumen that it can its bounden proteins that adapt the actions; phosphoric acerbic is removed, it is a about-face activity (if activated by phosphorylation, dephosphorylation is to arrest the effect), phosphatase actuality played an important role. The role of protein phosphatases and protein kinases opposite. According to dephosphorylation of altered amino acerbic residues, is aswell disconnected into protein phosphatase protein tyrosine phosphatase (PTP, PTPase) and serine / threonine phosphatases. Complex in lymphocyte activation of protein phosphatases are: ① CD45: The atomic anatomy of the intracellular domains of the two segments to play the role of PTP, and appropriately accord to CD45 receptor-type protein tyrosine phosphatase, beat kPTK role in the action adjoin aqueous and startup cellular arresting transduction plays a key role; ② calcineurin (calcineurin) is a serine / threonine phosphatase, its substrate is the archetype agency NF-AT atom has occurred phosphorylated serine and threonine residues. Calcineurin in the role, NF-ATp due to abatement of phosphate (p) and the activation, a archetype agency activating NF-AT.

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