Phosphorylation

Phosphorylated residue.

Phosphorylation(Lin-san ?,: phosphorylation) is to add various, especially above all. This reaction plays a major role in, and as of February, there are over 210,000 articles on database protein phosphorylation.

Phosphorylation is also called"phosphorylation". Enzymes that catalyze phosphorylation are generally (Kinase) In particular, it is often called simply as a kinase that a protein is a substrate.

Sometimes, biosynthesis (phosphorylation to phosphorylation) is sometimes simply referred to as phosphorylation ("," etc.).

table of contents

Protein phosphorylation

History

(Phoebus A. T. Levene) However, it was confirmed that there was protein (,) in (USA). And, by the same time, we found out that there was inside. However, it took another 20 years before the first announcement of "protein phosphorylation by enzymes".

reaction

Reversible phosphorylation of proteins is an important regulatory mechanism present in both. This process is related to (phosphorylation) and (dephosphorylation) is called. Many enzymes and receptors are put in and out by phosphorylation and dephosphorylation. As a result, reversible phosphorylation leads to many and activate or deactivate them. Phosphorylation usually occurs in the,, and residues of eukaryotic proteins. In addition to serine, threonine, tyrosine residues, phosphorylation also occurs at the residue of the protein ,,,. The addition of phosphoric acid to amino acid residues with R polarity can extremely reverse the part within the protein. In this pathway, structural changes of proteins can be introduced through the interaction of hydrophobic and hydrophilic residues of other proteins.

As an example of regulation of phosphorylation, is. The regulation of p53 protein is very numerous and contains more than 18 phosphorylation sites. Activated p53 suppresses the progression of (or reverses depending on several factors) and can lead to cell death. This activity state only occurs if the condition of is damaged or the physiological function interferes with an ordinary individual.

At the deactivation signal, the protein is dephosphorylated again and stops its action. This is a mechanism of many types, for example the process by which light is processed by photosensitive cells of the retina.

Regulatory action including phosphorylation

Requires reaction energy

Phosphorylation of aspartic acid residues during transport of ion and ions through cell membranes for maintenance of body water content Mediation

Enzyme phosphorylation by a part of (protein kinase B) Phosphorylation of src tyrosine kinase (sarc) by the C-terminal Src kinase (Csk) induces a structural change among its enzymes, with the mask of the kinase domain being wrapped in a closed state. Important via "recognition"

Phosphorylation of NADPH oxidase immobilized on the cytoplasmic constituent cell membrane. Current multiprotein enzymes play an important enzyme role in regulating protein-protein interactions of action. Importance of

In the late 1990s, phosphorylation of several proteins was observed in the dependent / pathway. These target proteins become substrates for E3 synthase only during phosphorylation.

Other phosphorylation

As soon as phosphorylation takes place, it is formed. This phosphorylation is to prevent glucose from diffusing out of the cell. Because charge is introduced by phosphorylation, glucose-6-phosphate can not easily pass through. Phosphorylated glucose enters metabolic pathways such as.

For details, see

Source

1. *P. A. Levene and C. L. Alsberg, The cleavage products of vitellin, J. Biol. Chem. 2 (1906), pp. 127-133. 2. F. A. Lipmann and P. A. Levene, Serine Phosphoric Acid Obtained on hydrolysis of vitellinic acid, _J. Biol. Chem. - 98 (1932), pp. 109-114. 3. *G. Burnett and E. P. Kennedy, The enzymatic phosphorylation of proteins, J. Biol. Chem. 211 (1954), pp. 969 - 980. 4. ^ A. J. Cozzon (1988) Protein phosphorylation in prokaryotes _ Ann. Rev. Microbiol. 42: 97- 125 5. ^ J. B. Stock, A. J. Ninfa and A. M. Stock (1989) Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. -, p. 450-490 6. C. Chang and R. C. Stewart (1998) The Two-Component System. Plant Physiol.. 117: 723-731 7. *D. Barford, A. K. Das and MP. Egloff. (1998) The Structure and mechanism of protein phosphatases: Insights into Catalysis and Regulation _ Annu Rev Biophys Biomol Struct. _ Vol. 27: 133-164 8. M. Ashcroft, M. H. G. Kubbutat, and K. H. Vousden (1999). Regulation of p53 Function and Stability by Phosphorylation. _Mol Cell Biol Mar; 19 (3): 1751-8. 9. *S. Bates, and K. H. Vousden. (1996). P53 in signalling checkpoint arrest or apoptosis. Curr. Opin. Genet. Dev. 6: 1-7. 10. PC van Weeren, KM de Bruyn, AM de Vries-Smits, J. Van Lint, BM Burgering. (1998). "Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J Biol Chem ~ 22; 273 (21): 13150-6. 11. *Cole, PA, Shen, K., Qiao, Y., and Wang, D. (2003) Protein tyrosine kinases Src and Csk: A tail's tale, Curr. Opin. Chem. , Biol. 7 : 580-585. 12. *, (1999). NADPH oxidase: an update. _ Blood _ 93, pp. 1464 - 1476

Related item

• • • • • • ·: Means phosphorylation, that is, synthesis reaction. *: Functional small molecule developed by the Drug Function Science Laboratory and a new phosphorylated bioanalytical analysis technology using it.

External link

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Post Date : 2018-02-04 00:00

This article is taken from the Japanese Wikipedia Phosphorylation

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