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Titolo:
THE STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS-MOBILIS - AN OSMOPROTECTIVE PERIPLASMIC ENZYME-CONTAINING NON-DISSOCIABLE NADP
Autore:
KINGSTON RL; SCOPES RK; BAKER EN;
Indirizzi:
MASSEY UNIV,DEPT BIOCHEM PALMERSTON NORTH NEW ZEALAND MASSEY UNIV,DEPT BIOCHEM PALMERSTON NORTH NEW ZEALAND LA TROBE UNIV,SCH BIOCHEM BUNDOORA VIC 3083 AUSTRALIA
Titolo Testata:
Structure
fascicolo: 12, volume: 4, anno: 1996,
pagine: 1413 - 1428
SICI:
0969-2126(1996)4:12<1413:TSOGOF>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ALDOSE REDUCTASE; 3-DIMENSIONAL STRUCTURE; LACTATE-DEHYDROGENASE; SORBITOL PRODUCTION; PROTEIN-STRUCTURE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; RESOLUTION; REFINEMENT; BINDING;
Keywords:
CRYSTAL STRUCTURE; NADP BINDING; OSMOTIC PROTECTION; OXIDOREDUCTASE; PERIPLASM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
79
Recensione:
Indirizzi per estratti:
Citazione:
R.L. Kingston et al., "THE STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS-MOBILIS - AN OSMOPROTECTIVE PERIPLASMIC ENZYME-CONTAINING NON-DISSOCIABLE NADP", Structure, 4(12), 1996, pp. 1413-1428

Abstract

Background: The organism Zymomonas mobilis occurs naturally in sugar-rich environments. To protect the bacterium against osmotic shock, theperiplasmic enzyme glucose-fructose oxidoreductase (GFOR) produces the compatible, solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone. Hence, Z, mobilis can tolerate high concentrations of sugars and this property may be useful in the development of an efficient microbial process for ethanol production, Each enzyme subunit contains tightly associated NADP which is not released during the catalytic cycle. Results: The structure of GFOR wasdetermined by X-ray crystallography at 2.7 Angstrom resolution, Each subunit of the tetrameric enzyme comprises two domains, a classical dinucleotide-binding domain, and a C-terminal domain based on a predominantly antiparallel nine-stranded beta sheet. In the tetramer, the subunits associate to form two extended 18-stranded beta sheets, which pack against each other in a face to face fashion, creating an extensive interface at the core of the tetramer, An N-terminal arm from each subunit wraps around the dinucleotide-binding domain of an adjacent subunit, covering the adenine ring of NADP. Conclusions: In GFOR, the NADP is found associated with a classical dinucleotide-binding domain in a conventional fashion, The NADP is effectively buried in the protein-subunit interior as a result of interactions with the N-terminal arm from an adjacent subunit in the tetramer, and with a short helix from theC-terminal domain of the protein, This accounts for NADP's inability to dissociate, The N-terminal arm may also contribute to stabilizationof the tetramer, The enzyme has an unexpected structural similarity with the cytoplasmic enzyme glucose-6-phosphate dehydrogenase (G6PD), We hypothesize that both enzymes have diverged from a common ancestor,The mechanism of catalysis is still unclear, but we have identified a conserved structural motif (Glu-Lys-Pro) in the active site of GFOR andG6PD that may be important for catalysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:23:11