Phosphopantetheine adenylyltransferase
Short name | PPAT |
Overlapping homologous superfamilies |
Description
References
1.Phosphopantetheine adenylyltransferase from Escherichia coli: investigation of the kinetic mechanism and role in regulation of coenzyme A biosynthesis. Miller JR, Ohren J, Sarver RW, Mueller WT, de Dreu P, Case H, Thanabal V. J. Bacteriol. 189, 8196-205, (2007). View articlePMID: 17873050
2.CTP:phosphocholine cytidylyltransferase: insights into regulatory mechanisms and novel functions. Clement JM, Kent C. Biochem. Biophys. Res. Commun. 257, 643-50, (1999). View articlePMID: 10208837
3.The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity. Izard T, Geerlof A. EMBO J. 18, 2021-30, (1999). View articlePMID: 10205156
4.A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing. Clementz T, Raetz CR. J. Biol. Chem. 266, 9687-96, (1991). View articlePMID: 2033061
5.The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism. Izard T. J. Mol. Biol. 315, 487-95, (2002). View articlePMID: 11812124
6.Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. Geerlof A, Lewendon A, Shaw WV. J. Biol. Chem. 274, 27105-11, (1999). View articlePMID: 10480925
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties