[CAPP_ECOLI] Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.[HAMAP-Rule:MF_00595]
Evolutionary Conservation
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Publication Abstract from PubMed
We have determined the crystal structure of Mn2+-bound Escherichia coli phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A resolution, and specified the location of enzyme-bound Mn2+, which is essential for catalytic activity. The electron density map reveals that Mn2+ is bound to the side chain oxygens of Glu-506 and Asp-543, and located at the top of the alpha/beta barrel in PEPC. The coordination sphere of Mn2+ observed in E. coli PEPC is similar to that of Mn2+ found in the pyruvate kinase structure. The model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.
Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli.,Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y FEBS Lett. 1999 Sep 17;458(2):93-6. PMID:10481043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y. Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli. FEBS Lett. 1999 Sep 17;458(2):93-6. PMID:10481043
