Abstract
ORF MJ1605, previously annotated as pgi and coding for the putative glucose-6-phosphate isomerase (phosphoglucose isomerase, PGI) of the hyperthermophilic archaeon Methanococcus jannaschii, was cloned and functionally expressed in Escherichia coli. The purified 80-kDa protein consisted of a single subunit of 45 kDa, indicating a homodimeric (alpha(2)) structure. The K(m) values for fructose 6-phosphate and glucose 6-phosphate were 0.04 mM and 1 mM, the corresponding V(max) values were 20 U/mg and 9 U/mg, respectively (at 50 degrees C). The enzyme had a temperature optimum at 89 degrees C and showed significant thermostability up to 95 degrees C. The enzyme was inhibited by 6-phosphogluconate and erythrose-4-phosphate. RT-PCR experiments demonstrated in vivo expression of ORF MJ1618 during lithoautotrophic growth of M. jannaschii on H(2)/CO(2). Phylogenetic analyses indicated that M. jannaschii PGI was obtained from bacteria, presumably from the hyperthermophile Thermotoga maritima.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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Dimerization
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Enzyme Inhibitors / pharmacology
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Enzyme Stability
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Escherichia coli / genetics
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Gene Expression Regulation, Archaeal
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Gluconates / metabolism
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Glucose-6-Phosphate Isomerase / chemistry
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Glucose-6-Phosphate Isomerase / genetics*
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Glucose-6-Phosphate Isomerase / isolation & purification
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Glucose-6-Phosphate Isomerase / metabolism*
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Methanococcus / enzymology*
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Methanococcus / genetics*
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Molecular Weight
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Phylogeny
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Protein Subunits / chemistry
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Protein Subunits / metabolism
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RNA, Messenger / analysis
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Reverse Transcriptase Polymerase Chain Reaction
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Sugar Phosphates / metabolism
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Temperature
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Transcription, Genetic
Substances
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Enzyme Inhibitors
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Gluconates
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Protein Subunits
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RNA, Messenger
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Recombinant Proteins
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Sugar Phosphates
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erythrose 4-phosphate
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Glucose-6-Phosphate Isomerase
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6-phosphogluconic acid