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Function
Phosphotransferase (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair of groups. PT which phosphoryltes six-carbon sugars is called Hexokinase. Adenylate kinase 3 (AK3) is a GTP:ATP PT.
- 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].
- Microlide 2”-phosphotransferase inactivates erythroycin[4].
- Polyphosphate:AMP phosphotransferase catalyzes phosphorylation of AMP to ADP[5].
- tRNA 2'- phosphotransferase catalyzes the removl of 2'-phosphate at tRNA splice junctions[6].
See:
Structural highlights
The active site of amino glycoside PT is located at a structural cleft and contains the aspartate catalytic base[7]. Water molecules are shown as red spheres.
3D structures of phosphotransferase
Phosphotransferase 3D structures
- ↑ Wright GD, Thompson PR. Aminoglycoside phosphotransferases: proteins, structure, and mechanism. Front Biosci. 1999 Jan 1;4:D9-21. PMID:9872733
- ↑ 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:https://dx.doi.org/10.1371/journal.pone.0150320
- ↑ 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
- ↑ 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
- ↑ Shiba T, Itoh H, Kameda A, Kobayashi K, Kawazoe Y, Noguchi T. Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A. J Bacteriol. 2005 Mar;187(5):1859-65. PMID:15716459 doi:https://dx.doi.org/10.1128/JB.187.5.1859-1865.2005
- ↑ Ghosh S, Dantuluri S, Jacewicz A, Sanchez AM, Abdullahu L, Damha MJ, Schwer B, Shuman S. Characterization of tRNA splicing enzymes RNA ligase and tRNA 2'-phosphotransferase from the pathogenic fungi Mucorales. RNA. 2024 Mar 18;30(4):367-380. PMID:38238085 doi:10.1261/rna.079911.123
- ↑ 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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