title: Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs.
abstract: In this paper we report the amino acid sequence of pyruvate phosphate dikinase (PPDK) from Bacteroides symbiosus as determined from the nucleotide sequence of the PPDK gene. Comparison of the B. symbiosus PPDK amino acid sequence with that of the maize PPDK [Matsuoka, M., Ozeki, Y., Yamamoto, N., Hirano, H., Kamo-Murakami, Y., & Tanaka, Y. (1988) J. Biol. Chem. 263, 11080] revealed long stretches of homologous sequence (greater than 70% identity), which contributed to an overall sequence identity of 53%. The circular dichrosim spectra, hydropathy profiles, and calculated secondary structural elements of the two dikinases suggest that they may have very similar tertiary structures as well. A comparison made between the amino acid sequence of the maize and B. symbiosus dikinase with other known protein sequences revealed homology, concentrated in three stretches of sequences, to a mechanistically related enzyme, enzyme I of the Escherichia coli PEP: sugar phosphotransferase system [Saffen, D. W., Presper, K. A., Doering, T. L., Roseman, S. (1987) J. Biol. Chem. 262, 16241]. It is proposed that (i) these three stretches of sequence constitute the site for PEP binding and catalysis and a possible site for the regulation of enzymatic activity and (ii) the conserved sequences exist in a third mechanistically related enzyme, PEP synthase.
authors.affiliation: Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.
authors.forename: D J
authors.initials: DJ
authors.lastname: Pocalyko
authors.forename: L J
authors.initials: LJ
authors.lastname: Carroll
authors.forename: B M
authors.initials: BM
authors.lastname: Martin
authors.forename: P C
authors.initials: PC
authors.lastname: Babbitt
authors.forename: D
authors.initials: D
authors.lastname: Dunaway-Mariano
mesh_terms: D000595:Amino Acid Sequence; D001439:Bacteroides / Q000201:enzymology*; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D002942:Circular Dichroism; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010944:Plants / Q000201:enzymology*; D010957:Plasmids; D011487:Protein Conformation; D011772:Pyruvate, Orthophosphate Dikinase / Q000737:chemistry / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D003313:Zea mays
chemical_list: D004269:DNA, Bacterial; D010446:Peptide Fragments; D011772:Pyruvate, Orthophosphate Dikinase; D004262:DNA Restriction Enzymes