PMID- 20044937
OWN - NLM
STAT- MEDLINE
DCOM- 20100506
LR  - 20211020
IS  - 1471-2091 (Electronic)
IS  - 1471-2091 (Linking)
VI  - 11
DP  - 2010 Jan 3
TI  - Cloning and characterization of Escherichia coli DUF299: a bifunctional 
      ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria.
PG  - 1
LID - 10.1186/1471-2091-11-1 [doi]
AB  - BACKGROUND: Phosphoenolpyruvate synthetase (PEPS; EC 2.7.9.2) catalyzes the 
      synthesis of phosphoenolpyruvate from pyruvate in Escherichia coli when cells are 
      grown on a three carbon source. It also catalyses the anabolic conversion of 
      pyruvate to phosphoenolpyruvate in gluconeogenesis. A bioinformatics search 
      conducted following the successful cloning and expression of maize leaf pyruvate, 
      orthophosphate dikinase regulatory protein (PDRP) revealed the presence of PDRP 
      homologs in more than 300 bacterial species; the PDRP homolog was identified as 
      DUF299. RESULTS: This paper describes the cloning and expression of both PEPS and 
      DUF299 from E. coli and establishes that E. coli DUF299 catalyzes both the 
      ADP-dependent inactivation and the Pi-dependent activation of PEPS. CONCLUSION: 
      This paper represents the first report of a bifunctional regulatory enzyme 
      catalysing an ADP-dependent phosphorylation and a Pi-dependent 
      pyrophosphorylation reaction in bacteria.
FAU - Burnell, Jim N
AU  - Burnell JN
AD  - Department of Biochemistry and Molecular Biology, James Cook University, 
      Townsville, Queensland 4811, Australia. James.Burnell@jcu.edu.au
LA  - eng
PT  - Journal Article
DEP - 20100103
PL  - England
TA  - BMC Biochem
JT  - BMC biochemistry
JID - 101084098
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Multienzyme Complexes)
RN  - 61D2G4IYVH (Adenosine Diphosphate)
RN  - 73-89-2 (Phosphoenolpyruvate)
RN  - 8558G7RUTR (Pyruvic Acid)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.33 (DUF299 protein, E coli)
RN  - EC 2.7.9.- (Phosphotransferases (Paired Acceptors))
RN  - EC 2.7.9.1 (Pyruvate, Orthophosphate Dikinase)
RN  - EC 2.7.9.2 (pyruvate, water dikinase)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
SB  - IM
MH  - Adenosine Diphosphate/*metabolism
MH  - Cloning, Molecular
MH  - Escherichia coli/*enzymology
MH  - Escherichia coli Proteins/classification/genetics/*metabolism
MH  - Gluconeogenesis
MH  - Multienzyme Complexes/classification/genetics/*metabolism
MH  - Phosphoenolpyruvate/metabolism
MH  - Phosphoric Monoester Hydrolases/classification/genetics/*metabolism
MH  - Phosphotransferases (Paired Acceptors)/classification/genetics/*metabolism
MH  - Phylogeny
MH  - Protein Kinases/classification/genetics/*metabolism
MH  - Pyruvate, Orthophosphate Dikinase/classification/genetics/metabolism
MH  - Pyruvic Acid/metabolism
MH  - Zea mays/enzymology
PMC - PMC2817694
EDAT- 2010/01/05 06:00
MHDA- 2010/05/07 06:00
PMCR- 2010/01/03
CRDT- 2010/01/05 06:00
PHST- 2009/09/10 00:00 [received]
PHST- 2010/01/03 00:00 [accepted]
PHST- 2010/01/05 06:00 [entrez]
PHST- 2010/01/05 06:00 [pubmed]
PHST- 2010/05/07 06:00 [medline]
PHST- 2010/01/03 00:00 [pmc-release]
AID - 1471-2091-11-1 [pii]
AID - 10.1186/1471-2091-11-1 [doi]
PST - epublish
SO  - BMC Biochem. 2010 Jan 3;11:1. doi: 10.1186/1471-2091-11-1.