Molecular characterization of phosphoglycerate mutase in archaea

The interconversion of 3-phosphoglycerate and 2-phosphoglycerate during glycolysis and gluconeogenesis is catalyzed by phosphoglycerate mutase (PGM). In bacteria and eukaryotes two structurally distinct enzymes have been found, a cofactor-dependent and a cofactor-independent (iPGM) type. Sequence an...

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Bibliographic Details
Published in:FEMS microbiology letters 2002-06, Vol.212 (1), p.111-120
Main Authors: van der Oost, John, Huynen, Martijn A., Verhees, Corné H.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Archaea - enzymology
Archaea - genetics
Archaeon
Bacteriology
Biological and medical sciences
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli - growth & development
Fundamental and applied biological sciences. Psychology
Genetics
Glycolysis
Laboratorium voor Microbiologie
Metabolism. Enzymes
Methanococcus
Methanococcus - enzymology
Methanococcus - genetics
Methanococcus - growth & development
Microbiological Laboratory
Microbiologie
Microbiology
Molecular Sequence Data
Phosphoglycerate mutase
Phosphoglycerate Mutase - chemistry
Phosphoglycerate Mutase - genetics
Phosphoglycerate Mutase - metabolism
Phylogeny
Pyrococcus
Pyrococcus furiosus - enzymology
Pyrococcus furiosus - genetics
Pyrococcus furiosus - growth & development
Sequence Alignment
Substrate Specificity
VLAG
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Summary:The interconversion of 3-phosphoglycerate and 2-phosphoglycerate during glycolysis and gluconeogenesis is catalyzed by phosphoglycerate mutase (PGM). In bacteria and eukaryotes two structurally distinct enzymes have been found, a cofactor-dependent and a cofactor-independent (iPGM) type. Sequence analysis of archaeal genomes did not find PGMs of either kind, but identified a new family of proteins, distantly related to iPGMs. In this study, these predicted archaeal PGMs from Pyrococcus furiosus and Methanococcus jannaschii have been functionally produced in Escherichia coli, and characterization of the purified proteins has confirmed that they are iPGMs. Analysis of the available microbial genomes indicates that this new type of iPGM is widely distributed among archaea and also encoded in several bacteria. In addition, as has been demonstrated in certain bacteria, some archaea appear to possess an alternative, cofactor-dependent PGM.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(02)00720-6