The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP

Kingston, Richard L.; Scopes, Robert K.; Baker, Edward N.

doi:10.1016/s0969-2126(96)00149-9

Cited by 85 publications

(116 citation statements)

References 70 publications

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“…2a) demonstrates that these two proteins superimpose with a rootmean-square deviation of 2.0 Å for 307 structurally equivalent ␣-carbons, which is remarkable given their limited amino acid sequence identity of ϳ13% (16). It has been postulated that Lys-129 and Tyr-217 are involved in the catalytic mechanism of the oxidoreductase (13). These residues correspond to Trp-123 and His-214 in KlGal80p.…”

Section: Resultsmentioning

confidence: 87%

Understanding a Transcriptional Paradigm at the Molecular Level

Thoden

Sellick

Reece

et al. 2007

Journal of Biological Chemistry

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In yeast, the GAL genes encode the enzymes required for normal galactose metabolism. Regulation of these genes in response to the organism being challenged with galactose has served as a paradigm for eukaryotic transcriptional control over the last 50 years. Three proteins, the activator Gal4p, the repressor Gal80p, and the ligand sensor Gal3p, control the switch between inert and active gene expression. Gal80p, the focus of this investigation, plays a pivotal role both in terms of repressing the activity of Gal4p and allowing the GAL switch to respond to galactose. Here we present the three-dimensional structure of Gal80p from Kluyveromyces lactis and show that it is structurally homologous to glucose-fructose oxidoreductase, an enzyme in the sorbitol-gluconate pathway. Our results clearly define the overall tertiary and quaternary structure of Gal80p and suggest that Gal4p and Gal3p bind to Gal80p at distinct but overlapping sites. In addition to providing a molecular basis for previous biochemical and genetic studies, our structure demonstrates that much of the enzymatic scaffold of the oxidoreductase has been maintained in Gal80p, but it is utilized in a very different manner to facilitate transcriptional regulation.

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Section: Resultsmentioning

confidence: 87%

Understanding a Transcriptional Paradigm at the Molecular Level

Thoden

Sellick

Reece

et al. 2007

Journal of Biological Chemistry

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“…Especially AAOR catalyzes also the reactions of a panel of different sugars. 4,5 GP6D is more specific, it catalyses oxidation (dehydrogenation) of D-glucose-6-phosphate to 6-phospho-D-glucono-1,5-lactone. 1 AFR reduces C2 carbon of 1,5-anhydro-Dfructose, the central intermediate of the anhydrofructose pathway.…”

Section: Catalyzed Reactionsmentioning

confidence: 99%

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases

2016

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The Gfo/Idh/MocA protein family contains a number of different proteins, which almost exclusively consist of NAD(P)-dependent oxidoreductases that have a diverse set of substrates, typically pyranoses. In this study, to clarify common structural features that would contribute to their function, the available crystal structures of the members of this family have been analyzed. Despite a very low sequence identity, the central features of the three-dimensional structures of the proteins are surprisingly similar. The members of the protein family have a two-domain structure consisting of a N-terminal nucleotide-binding domain and a C-terminal a/b-domain. The C-terminal domain contributes to the substrate binding and catalysis, and contains a ba-motif with a central a-helix carrying common essential amino acid residues. The b-sheet of the a/b-domain contributes to the oligomerization in most of the proteins in the family.

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“…Site-directed mutagenesis and X-ray crystallographic studies [46,47] have revealed that this enzyme has a typical dinucleotide-binding domain, i.e. a Rossmann (β-α-β) fold [48] with a fingerprint sequence, an N-terminal Gly-Xaa-Gly-Xaa-Xaa-Ala sequence and a Glu-Lys-Pro motif for interaction with the carboxamide group of the nicotinamide ring and the nicotinamide ribose.…”

Section: Alignment Of Dimeric Dds With Other Proteinsmentioning

confidence: 99%

“…However, because the secondary structures of the proteins listed in Figure 2 predicted the β-α-β-fold around the N-terminal regions from Gly-6 to Gly-11 of dimeric DDs (results not shown), it is possible that dimeric DD also has a coenzymebinding domain composed of the N-terminal β-α-β fold and the Glu-Lys-Pro motif. However, the substrate-binding domain of GFO has not been elucidated but two residues, Tyr-217 and Tyr-296, have been proposed as candidates for the catalytic residue on the basis of the three-dimensional structure of the enzyme [47]. Of these, only Tyr-217 is conserved at position 180 of dimeric DDs and the proteins in Figure 2, but is not present in the other proteins listed in Table 3.…”

Section: Alignment Of Dimeric Dds With Other Proteinsmentioning

confidence: 99%

Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases

Arimitsu

Aoki

Ishikura

et al. 1999

Biochemical Journal

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Cynomolgus and Japanese monkey kidneys, dog and pig livers and rabbit lens contain dimeric dihydrodiol dehydrogenase (EC 1.3.1.20) associated with high carbonyl reductase activity. Here we have isolated cDNA species for the dimeric enzymes by reverse transcriptase-PCR from human intestine in addition to the above five animal tissues. The amino acid sequences deduced from the monkey, pig and dog cDNA species perfectly matched the partial sequences of peptides digested from the respective enzymes of these animal tissues, and active recombinant proteins were expressed in a bacterial system from the monkey and human cDNA species. Northern blot analysis revealed the existence of a single 1.3 kb mRNA species for the enzyme in these animal tissues. The human enzyme shared 94%, 85%, 84% and 82% amino acid identity with the enzymes of the two monkey strains (their sequences were identical), the dog, the pig and the rabbit respectively. The sequences of the primate enzymes consisted of 335 amino acid residues and lacked one amino acid compared with the other animal enzymes. In contrast with previous reports that other types of dihydrodiol dehydrogenase, carbonyl reductases and enzymes with either activity belong to the aldo-keto reductase family or the short-chain dehydrogenase/reductase family, dimeric dihydrodiol dehydrogenase showed no sequence similarity with the members of the two protein families. The dimeric enzyme aligned with low degrees of identity (14-25%) with several prokaryotic proteins, in which 47 residues are strictly or highly conserved. Thus dimeric dihydrodiol dehydrogenase has a primary structure distinct from the previously known mammalian enzymes and is suggested to constitute a novel protein family with the prokaryotic proteins.

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The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP

Cited by 85 publications

References 70 publications

Understanding a Transcriptional Paradigm at the Molecular Level

Understanding a Transcriptional Paradigm at the Molecular Level

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases

Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases

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