Phosphotransferase

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'''Phosphotransferase''' (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups.<br />
'''Phosphotransferase''' (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups.<br />
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* '''Aminoglycoside PT''' (AGPT) inactivate aminoglycoside antibiotics by phosphorylation.<br />
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* '''Aminoglycoside PT''' (AGPT) inactivate aminoglycoside antibiotics by phosphorylation<ref>PMID:9872733</ref>.<br />
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* '''Phosphoenolpyruvate-protein PT''' (PEP) catalyzes the phosphorylation of protein histidine residues.<br />
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* '''Phosphoenolpyruvate-protein PT''' (PEP) catalyzes the phosphorylation of protein histidine residues<ref>PMID:26990554</ref>.<br />
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* '''Sporulation initiation PT''' (Spo0B, Spo0F) are elements in the phosphorelay system which regulates the initiation of sporulation.<br />
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* '''Sporulation initiation PT''' (Spo0B, Spo0F) are elements in the phosphorelay system which regulates the initiation of sporulation<ref>PMID:1664534</ref>.<br />
See: <br />
See: <br />
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== References ==
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<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Revision as of 09:18, 3 July 2016

Template:STRUCTURE 3q2m

Phosphotransferase (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups.

  • Aminoglycoside PT (AGPT) inactivate aminoglycoside antibiotics by phosphorylation[1].
  • Phosphoenolpyruvate-protein PT (PEP) catalyzes the phosphorylation of protein histidine residues[2].
  • Sporulation initiation PT (Spo0B, Spo0F) are elements in the phosphorelay system which regulates the initiation of sporulation[3].

See:

3D structures of phosphotransferase

Updated on 03-July-2016

References

  1. Wright GD, Thompson PR. Aminoglycoside phosphotransferases: proteins, structure, and mechanism. Front Biosci. 1999 Jan 1;4:D9-21. PMID:9872733
  2. Mizrachi Nebenzahl Y, Blau K, Kushnir T, Shagan M, Portnoi M, Cohen A, Azriel S, Malka I, Adawi A, Kafka D, Dotan S, Guterman G, Troib S, Fishilevich T, Gershoni JM, Braiman A, Mitchell AM, Mitchell TJ, Porat N, Goliand I, Chalifa Caspi V, Swiatlo E, Tal M, Ellis R, Elia N, Dagan R. Streptococcus pneumoniae Cell-Wall-Localized Phosphoenolpyruvate Protein Phosphotransferase Can Function as an Adhesin: Identification of Its Host Target Molecules and Evaluation of Its Potential as a Vaccine. PLoS One. 2016 Mar 18;11(3):e0150320. doi: 10.1371/journal.pone.0150320., eCollection 2016. PMID:26990554 doi:http://dx.doi.org/10.1371/journal.pone.0150320
  3. Trach K, Burbulys D, Strauch M, Wu JJ, Dhillon N, Jonas R, Hanstein C, Kallio P, Perego M, Bird T, et al.. Control of the initiation of sporulation in Bacillus subtilis by a phosphorelay. Res Microbiol. 1991 Sep-Oct;142(7-8):815-23. PMID:1664534

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