Phosphotransferase

From Proteopedia

spinqualitylabelsall models Aminoglycoside phosphotransferase complex with gentamycin, and glycerol (PDB entry 3ham) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Structural highlights 3 3D structures of phosphotransferase 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]. See: Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System Enzyme I of the S. aureus PTS User:Karl Oberholser/Phosphoenolpyruvate:Sugar Phosphotransferase for a flash movie. Structural highlights The is located at a structural cleft and contains the [6]. Water molecules are shown as red spheres. 3D structures of phosphotransferase Phosphotransferase 3D structures

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. ↑ 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:http://dx.doi.org/10.1128/JB.187.5.1859-1865.2005
6. ↑ 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