Phosphorylation | Wikipedia audio article
Channel: wikipedia tts
Date: 10/05/2019

This is an audio version of the Wikipedia Article:
https://en.wikipedia.org/wiki/Phosphorylation


00:02:10 1 Glucose
00:06:08 2 Protein phosphorylation
00:06:19 2.1 Function
00:12:31 2.2 Signaling networks
00:13:59 2.3 Types of phosphorylation
00:15:38 2.4 Phosphorylation of histones
00:17:43 2.5 Detection and characterization
00:21:27 3 ATP
00:22:07 4 See also



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SUMMARY
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In chemistry, phosphorylation of a molecule is the attachment of a phosphoryl group.  Together with its counterpart, dephosphorylation, it is critical for many cellular processes in biology. Phosphorylation is especially important for protein function; for example, this modification activates (or deactivates) almost half of the enzymes present in yeast, thereby regulating their function. Many proteins (between 1/3 to 2/3 of the proteome in eukaryotes) are phosphorylated temporarily, as are many sugars, lipids, and other molecules.
Protein phosphorylation is considered the most abundant post-translational modification in eukaryotes. Phosphorylation can occur on serine, threonine and tyrosine side chains (often called 'residues') through phosphoester bond formation, on histidine, lysine and arginine through phosphoramidate bonds, and on aspartic acid and glutamic acid through mixed anhydride linkages. Recent evidence confirms widespread histidine phosphorylation at both the 1 and 3 N-atoms of the imidazole ring Recent work from 2017 (preprinted at BioRxiv) suggests widespread human protein phosphorylation on multiple non-canonical amino acids, including motifs containing phosphorylated histidine, aspartate, glutamate, arginine and lysine in HeLa cell extracts. Due to the chemical lability of these phosphorylated residues, and in marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated histidine using standard biochemical and mass spectrometric approaches is much more challenging and special procedures and separation techniques are required for their preservation alongside classical Ser, Thr and Tyr phosphorylation.The prominent role of protein phosphorylation in biochemistry is illustrated by the huge body of studies published on the subject (as of March 2015, the MEDLINE database returns over 240,000 articles, mostly on protein phosphorylation).