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PROSITE documentation PDOC00460

Phosphoenolpyruvate carboxykinase (ATP) signature





Description

Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49) (PEPCK) [1] catalyzes the formation of phosphoenolpyruvate by decarboxylation of oxaloacetate while hydrolyzing ATP, a rate limiting step in gluconeogenesis (the biosynthesis of glucose).

The sequence of this enzyme has been obtained from Escherichia coli, yeast, and Trypanosoma brucei; these three sequences are evolutionary related and share many regions of similarity. As a signature pattern we selected a highly conserved region that contains four acidic residues and which is located in the central part of the enzyme. The beginning of the pattern is located about 10 residues to the C-terminus of an ATP-binding motif 'A' (P-loop) (see <PDOC00017>) and is also part of the ATP-binding domain [2].

Note:

Phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) an enzyme that catalyzes the same reaction, but using GTP instead of ATP, is not related to the above enzyme (see <PDOC00421>).

Last update:

April 2006 / Pattern revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

PEPCK_ATP, PS00532; Phosphoenolpyruvate carboxykinase (ATP) signature  (PATTERN)


References

1AuthorsMedina V. Pontarollo R. Glaeske D. Tabel H. Goldie H.
TitleSequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae.
SourceJ. Bacteriol. 172:7151-7156(1990).
PubMed ID1701430

2AuthorsMatte A. Goldie H. Sweet R.M. Delbaere L.T.J.
TitleCrystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold.
SourceJ. Mol. Biol. 256:126-143(1996).
PubMed ID8609605



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