Literature: Phosphoenolpyruvate carboxylase, Lys active site (IPR018129)
References used in this entry
The following publications were referred to in the abstract:
Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction.
Terada K, Izui K.
Eur. J. Biochem. 202 797-803 1991
PMID: 1765093 Related citations
Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate.
Jiao JA, Podesta FE, Chollet R, O'Leary MH, Andreo CS.
Biochim. Biophys. Acta 1041 291-5 1990
PMID: 2268676 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
Kai Y, Matsumura H, Inoue T, Terada K, Nagara Y, Yoshinaga T, Kihara A, Tsumura K, Izui K.
Proc. Natl. Acad. Sci. U.S.A. 96 823-8 1999
PMID: 9927652 Related citations
Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.
Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y.
Structure 10 1721-30 2002
PMID: 12467579 Related citations
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. 458 93-6 1999
PMID: 10481043 Related citations