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Your search keyword '"Triose-Phosphate Isomerase isolation & purification"' showing total 4 results
Start Over Descriptor "Triose-Phosphate Isomerase isolation & purification" Topic multienzyme complexes
4 results on '"Triose-Phosphate Isomerase isolation & purification"'

1. Phosphoglycerate kinases from bacteria and archaea.

Author

Crowhurst G, McHarg J, and Littlechild JA

Subjects
Amino Acid Sequence, Archaea enzymology, Chromatography, Gel methods, Chromatography, Ion Exchange methods, Cloning, Molecular, Conserved Sequence, Crystallization, Escherichia coli genetics, Models, Molecular, Molecular Sequence Data, Multienzyme Complexes isolation & purification, Phosphoglycerate Kinase isolation & purification, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins chemistry, Recombinant Proteins isolation & purification, Sequence Alignment, Sequence Homology, Amino Acid, Thermotoga maritima genetics, Thermus thermophilus genetics, Triose-Phosphate Isomerase isolation & purification, Bacterial Proteins, Geobacillus stearothermophilus enzymology, Multienzyme Complexes chemistry, Phosphoglycerate Kinase chemistry, Phosphoglycerate Kinase genetics, Thermotoga maritima enzymology, Thermus thermophilus enzymology, Triose-Phosphate Isomerase chemistry
Published
2001
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2. Phosphoglycerate kinase-triose-phosphate isomerase complex from Thermotoga neapolitana.

Author

Yu JS and Noll KM

Subjects
Cloning, Molecular, Conjugation, Genetic, Electrophoresis, Polyacrylamide Gel methods, Escherichia coli, Genomic Library, Gram-Negative Anaerobic Straight, Curved, and Helical Rods genetics, Hexokinase genetics, Kinetics, Molecular Weight, Multienzyme Complexes isolation & purification, Phosphoglycerate Kinase isolation & purification, Recombinant Fusion Proteins isolation & purification, Recombinant Fusion Proteins metabolism, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Triose-Phosphate Isomerase isolation & purification, Bacterial Proteins, Gram-Negative Anaerobic Straight, Curved, and Helical Rods enzymology, Multienzyme Complexes genetics, Multienzyme Complexes metabolism, Phosphoglycerate Kinase genetics, Phosphoglycerate Kinase metabolism, Triose-Phosphate Isomerase genetics, Triose-Phosphate Isomerase metabolism
Published
2001
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3. Quantitative two-dimensional gel electrophoresis: from proteins to proteomes.

Author

Dunn MJ

Subjects
Amino Acid Sequence, Amino Acids analysis, Cardiovascular System enzymology, Humans, Information Systems, Myocardium enzymology, Proteasome Endopeptidase Complex, Proteins chemistry, Reproducibility of Results, Software, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Triose-Phosphate Isomerase chemistry, Triose-Phosphate Isomerase isolation & purification, Cysteine Endopeptidases isolation & purification, Electrophoresis, Gel, Two-Dimensional methods, Multienzyme Complexes isolation & purification, Proteins isolation & purification
Published
1997
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4. Phosphoglycerate kinase and triosephosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex.

Author

Schurig H, Beaucamp N, Ostendorp R, Jaenicke R, Adler E, and Knowles JR

Subjects
Amino Acid Sequence, Base Sequence, Cloning, Molecular, Enzyme Stability genetics, Escherichia coli genetics, Genes, Bacterial genetics, Gram-Negative Anaerobic Bacteria enzymology, Hot Temperature, Hydrogen-Ion Concentration, Molecular Sequence Data, Molecular Weight, Multienzyme Complexes chemistry, Multienzyme Complexes isolation & purification, Multienzyme Complexes metabolism, Osmolar Concentration, Phosphoglycerate Kinase chemistry, Phosphoglycerate Kinase isolation & purification, Phosphoglycerate Kinase metabolism, Reading Frames genetics, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Recombinant Proteins biosynthesis, Sequence Analysis, Triose-Phosphate Isomerase chemistry, Triose-Phosphate Isomerase isolation & purification, Triose-Phosphate Isomerase metabolism, Gram-Negative Anaerobic Bacteria genetics, Multienzyme Complexes genetics, Phosphoglycerate Kinase genetics, Triose-Phosphate Isomerase genetics
Abstract

Phosphoglycerate kinase (PGK) from the hyperthermophilic bacterium Thermotoga maritima has been purified to homogeneity. A second larger enzyme with PGK activity and identical N-terminal sequence was also found. Surprisingly, this enzyme displayed triosephosphate isomerase (TIM) activity. No other TIM is detectable in T. maritima crude extracts. As shown by ultracentrifugal analysis, PGK is a 43 kDa monomer, whereas the bifunctional PGK-TIM fusion protein is a homotetramer of 240-285 kDa. SDS-PAGE indicated a subunit size of 70 kDa for the fusion protein. Both enzymes show high thermostability. Measurements of the catalytic properties revealed no extraordinary results. pH optima, Km values and activation energies were found to be in the range observed for other PGKs and TIMs investigated so far. The corresponding pgk and tpi genes are part of the apparent gap operon of T. maritima. This gene segment contains two overlapping reading frames, where the 43 kDa PGK is encoded by the upstream open reading frame, the pgk gene. On the other hand, the 70 kDa PGK-TIM fusion protein is encoded jointly by the pgk gene and the overlapping downstream open reading frame of the tpi gene. A programmed frameshift may be responsible for this fusion. A comparison of the amino acid sequence of both the PGK and the TIM parts of the fusion protein with those of known PGKs and TIMs reveals high similarity to the corresponding enzymes from different procaryotic and eucaryotic organisms.

Published
1995
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