Phosphotransferase

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* '''Phosphoenolpyruvate-protein PT''' (PEP) catalyzes the phosphorylation of protein histidine residues<ref>PMID:26990554</ref>.<br />
* '''Phosphoenolpyruvate-protein PT''' (PEP) catalyzes the phosphorylation of protein histidine residues<ref>PMID:26990554</ref>.<br />
* '''Sporulation initiation PT''' (Spo0B, Spo0F) are elements in the phosphorelay system which regulates the initiation of sporulation<ref>PMID:1664534</ref>.<br />
* '''Sporulation initiation PT''' (Spo0B, Spo0F) are elements in the phosphorelay system which regulates the initiation of sporulation<ref>PMID:1664534</ref>.<br />
 +
* '''Microlide 2”-phosphotransferase''' inactivates erythroycin<ref>PMID:10960087</ref>.<br />
See: <br />
See: <br />
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**[[3q15]] - BsPT spo0F + response regulator aspartate phosphatase<br />
**[[3q15]] - BsPT spo0F + response regulator aspartate phosphatase<br />
-
*Microlide 2”-phosphotransferase
+
*'''Microlide 2”-phosphotransferase'''
**[[5igh]] – EcMPT I <br />
**[[5igh]] – EcMPT I <br />
**[[5igi]], [[5igj]], [[5igs]], [[5igt]] – EcMPT I + antibiotic + guanosine<br />
**[[5igi]], [[5igj]], [[5igs]], [[5igt]] – EcMPT I + antibiotic + guanosine<br />
**[[5igp]], [[5igr]] – EcMPT I + antibiotic + GDP<br />
**[[5igp]], [[5igr]] – EcMPT I + antibiotic + GDP<br />
- 
**[[5uxa]], [[5igu]] – EcMPT II <br />
**[[5uxa]], [[5igu]] – EcMPT II <br />
**[[5uxb]] – BfMPT II – ''Brachybacterium faecium'' <br />
**[[5uxb]] – BfMPT II – ''Brachybacterium faecium'' <br />
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**[[5ih0]] – EcMPT II (mutant) + antibiotic + GDP<br />
**[[5ih0]] – EcMPT II (mutant) + antibiotic + GDP<br />
-
*Polyphospate:AMP phosphotransferase or polyphosphate kinase
+
*'''Polyphospate:AMP phosphotransferase or polyphosphate kinase'''
**[[5lc9]] – MrPAPT – ''Meiothermus ruber'' <br />
**[[5lc9]] – MrPAPT – ''Meiothermus ruber'' <br />

Revision as of 10:17, 6 September 2017

Aminoglycoside phosphotransferase complex with gentamycin, and glycerol (PDB entry 3ham)

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3D structures of phosphotransferase

Updated on 06-September-2017

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
  4. Noguchi N, Takada K, Katayama J, Emura A, Sasatsu M. Regulation of transcription of the mph(A) gene for macrolide 2'-phosphotransferase I in Escherichia coli: characterization of the regulatory gene mphR(A). J Bacteriol. 2000 Sep;182(18):5052-8. PMID:10960087
  5. Young PG, Walanj R, Lakshmi V, Byrnes LJ, Metcalf P, Baker EN, Vakulenko SB, Smith CA. The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2-phosphotransferase-IIa [APH(2)-IIa] provide insights into substrate selectivity in the APH(2) subfamily. J Bacteriol. 2009 Jul;191(13):4133-43. Epub 2009 May 8. PMID:19429619 doi:10.1128/JB.00149-09

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