PMID: 8584793Nov 1, 1995Paper

Phylogenetic analysis of the putative phosphorylation domain in the pyruvate kinase of Bacillus stearothermophilus

Research in Microbiology
C C Nguyen, Milton H Saier

Abstract

All sequenced phosphoenolpyruvate synthases (PPS), pyruvate:phosphate dikinases (PPDK) and enzymes I (EI) of the phosphoenolpyruvate:sugar phosphotransferase system comprise the PEP family. Linked to the C terminus of the sequenced pyruvate kinase from Bacillus stearothermophilus (PKBst) is a domain that is homologous to the putative phosphorylation domains of PEP family enzymes. We report sequence and phylogenetic analyses that lead to the following conclusions: (1) the phosphorylation domain of PKBst was derived from a PPS, late in the evolutionary process, after the divergence of PPSs from PPDKs and EIs; (2) this domain is probably functional in phosphoryl transfer; (3) the C-terminal phosphorylation domain in PKBst probably defines a compact domain in all PEP family proteins that is linked to other domains in these proteins via flexible linkers.

References

Jan 1, 1990·Methods in Enzymology·D F Feng, R F Doolittle
Sep 1, 1994·Molecular Microbiology·M H Saier, J Reizer

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Citations

Jun 1, 1997·Current Opinion in Structural Biology·J Reizer, M H Saier
Jun 12, 2003·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Ma Enriqueta Muñoz, Elizabeth Ponce
May 31, 2008·Journal of Biochemistry·Kenichiro SuzukiHiroshi Sakai
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Kenichiro SuzukiHiroshi Sakai
Dec 13, 2006·Microbiology and Molecular Biology Reviews : MMBR·Josef DeutscherPieter W Postma
Jun 6, 2000·Microbiology and Molecular Biology Reviews : MMBR·M H Saier
Dec 9, 2020·FEMS Microbiology Reviews·Jeroen G KoendjbiharieServé W M Kengen
May 7, 2021·FEMS Microbiology Reviews·Jeroen G KoendjbiharieServé W M Kengen

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