F
IPR001980

Phosphopantetheine adenylyltransferase

InterPro entry
Short namePPAT
Overlapping
homologous
superfamilies
 

Description

Phosphopantetheine adenylyltransferase (PPAT;
2.7.7.3
) is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis: catalysis of the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine to give dephospho-CoA (DPCOA) and pyrophosphate in the fourth (and penultimate) step of coenzyme A biosynthesis
[6]
. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases
[5, 3]
. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli
[2, 1]
.

The enzyme had previously been thought to have a role in lipopolysaccharide biosynthesis
[4]
.

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

Cross References

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.