| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10804189 | Biochimie | 2011 | 9 Pages |
Abstract
⺠Mannose-6-phosphate isomerase from T. thermophilus was characterized. ⺠The enzyme interconverted between mannose-6-phosphate and fructose-6-phosphate. ⺠The maximum activity of the enzyme was observed at pH 7.0 and 80 °C with 0.5 mM Zn2+. ⺠His50, Glu67, His122, and Glu132 of the enzyme were metal-binding residues. ⺠Arg11, Lys37, Gln48, Lys65, and Arg142 of the enzyme were substrate-binding residues.
Keywords
SDSThermus thermophilusEPPSPAGEFPLCIPTGpiperazine-N,N′-bis(2-ethanesulfonic acid)EDTAEthylenediaminetetraacetic acidpolyacrylamide gel electrophoresisisopropyl-β-d-thiogalactopyranosideCharacterizationGDPMolecular dynamicssodium dodecyl sulphatefast protein liquid chromatographyinductively coupled plasma mass spectrometryICP-MSLuria-BertaniPipesguanosine diphosphate
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Soo-Jin Yeom, Yeong-Su Kim, Yu-Ri Lim, Ki-Woong Jeong, Jee-Young Lee, Yangmee Kim, Deok-Kun Oh,