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A novel, cupin-type phosphoglucose isomerase in Escherichia coli.
Vorobjeva, Natalia N; Kurilova, Svetlana A; Petukhova, Anastasia F; Nazarova, Tatiana I; Kolomijtseva, Galina Ya; Baykov, Alexander A; Rodina, Elena V.
Afiliación
  • Vorobjeva NN; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
  • Kurilova SA; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
  • Petukhova AF; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
  • Nazarova TI; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
  • Kolomijtseva GY; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
  • Baykov AA; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
  • Rodina EV; Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia. Electronic address: rodina@belozersky.msu.ru.
Biochim Biophys Acta Gen Subj ; 1864(7): 129601, 2020 07.
Article en En | MEDLINE | ID: mdl-32179131
BACKGROUND: Escherichia coli cells contain a homolog of presumed 5-keto-4-deoxyuronate isomerase (KduI) from pectin-degrading soil bacteria, but the catalytic activity of the E. coli protein (o-KduI) was never demonstrated. METHODS: The known three-dimensional structure of E. coli o-KduI was compared with the available structures of sugar-converting enzymes. Based on the results of this analysis, sugar isomerization activity of recombinant o-KduI was tested against a panel of D-sugars and their derivatives. RESULTS: The three-dimensional structure of o-KduI exhibits a close similarity with Pyrococcus furiosus cupin-type phosphoglucose isomerase. In accordance with this similarity, o-KduI was found to catalyze interconversion of glucose-6-phosphate and fructose-6-phosphate and, less efficiently, conversion of glucuronate to fructuronate. o-KduI was hexameric in crystals but represented a mixture of inactive hexamers and active dimers in solution and contained a tightly bound Zn2+ ion. Dilution, substrate binding and Zn2+ removal shifted the hexamer ⇆ dimer equilibrium to the dimers. CONCLUSIONS: Our findings identify o-KduI as a novel phosphosugar isomerase in E. coli, whose activity may be regulated by changes in oligomeric structure. GENERAL SIGNIFICANCE: More than 5700 protein sequences are annotated as KduI, but their enzymatic activity has not been directly demonstrated. E. coli o-KduI is the first characterized member of this group, and its enzymatic activity was found to be different from the predicted activity.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Isomerasas Aldosa-Cetosa / Glucosa-6-Fosfato Isomerasa Tipo de estudio: Prognostic_studies Idioma: En Revista: Biochim Biophys Acta Gen Subj Año: 2020 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Isomerasas Aldosa-Cetosa / Glucosa-6-Fosfato Isomerasa Tipo de estudio: Prognostic_studies Idioma: En Revista: Biochim Biophys Acta Gen Subj Año: 2020 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Países Bajos