Crystal structure of the <i>Escherichia coli Tas</i> protein, an NADP(H)‐dependent aldo‐keto reductase

Obmolova, Galina; Teplyakov, A.; Khil, Pavel P.; Howard, Andrew; Camerini‐Otero, R. Daniel; Gilliland, Gary L.

doi:10.1002/prot.10367

Cited by 8 publications

(7 citation statements)

References 22 publications

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“…Indeed, enhanced accessibility to the active site appears to be a general feature of the AKR4C subfamily considering the crystal structure of barley aldose reductase (AKR4C1) and the primary sequences of other AKR4C enzymes. 47 Figure 5 shows a surface diagram of AKR4C8, AKR4C9, AKR1C3, 48 AKR7A2, 53 and Tas §, 55 generated using the programs Travel Depth 54 and PyMOL. 56 This representation enables a clear visualization of the substrate-and cofactor-binding sites.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Two Novel Aldo–Keto Reductases from Arabidopsis: Expression Patterns, Broad Substrate Specificity, and an Open Active-Site Structure Suggest a Role in Toxicant Metabolism Following Stress

Simpson

Tantitadapitak

Reed

et al. 2009

Journal of Molecular Biology

133

129

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Section: Discussionmentioning

confidence: 99%

Characterization of Two Novel Aldo–Keto Reductases from Arabidopsis: Expression Patterns, Broad Substrate Specificity, and an Open Active-Site Structure Suggest a Role in Toxicant Metabolism Following Stress

Simpson

Tantitadapitak

Reed

et al. 2009

Journal of Molecular Biology

133

129

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“…However, analysis of the crystal structure and X-ray data shows that this AKR is dimeric a fact ignored in the structure report [27], and contrary to the monomeric assignment by the authors in the PDB entry. Refinement and correction of the structure using the In forming a stable dimer, YgdS buries 1716 Å 2 of solvent accessible surface area, ~12% of the total solvent exposed surface of the protein (calculated using the program PISA [28]).…”

Section: A Dimeric Akr Ygds (B2834 Tas Protein)mentioning

confidence: 65%

The diversity of microbial aldo/keto reductases from Escherichia coli K12

Lapthorn

Zhu

Ellis

2013

Chemico-Biological Interactions

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reductase, tyrosine auxotrophy suppressor protein, L-glyceraldehyde 3-phosphate reductase, AKR quaternary structure. AbstractThe genome of Escherichia coli K12 contains 9 open reading frames encoding aldo/keto reductases (AKR) that are differentially regulated and sequence diverse. A significant amount of data is available for the E. coli AKRs through the availability of gene knockouts and gene expression studies, which adds to the biochemical and kinetic data.This together with the availability of crystal structures for nearly half of the E. coli AKRs and homologues of several others provides an opportunity to look at the diversity of these representative bacterial AKRs. Based around the common AKR fold of (β/α) 8 barrel with two additional α-helices, the E. coli AKRs have a loop structure that is more diverse than their mammalian counterparts, creating a variety of active site architectures. Nearly half of the AKRs are expected to be monomeric, but there are examples of dimeric, trimeric and octameric enzymes, as well as diversity in specificity for NAD as well as NADP as a cofactor. However in functional assignments and characterisation of enzyme activities there is a paucity of data when compared to the mammalian AKR enzymes. 1.

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“…They are further characterized by a conserved cofactor binding region for NAD(P)H, variable loop structures that define substrate specificity, and a catalytic tetrad (Hyndman et al, 2003; Jez et al, 1997; Penning, 2015). Of the 16 families of AKRs (Penning, 2015), only three dimeric AKRs have been reported: a rat liver aflatoxin dialdehyde reductase (AKR7A1), the Candida tenuis NAD(P)H dependent xylose reductase (AKR2B5), and the Escherichia coli tyrosine auxotrophy suppressor protein (Kavanagh et al, 2003; Kozma et al, 2002; Obmolova et al, 2003). The crystal structures of these proteins shows a conserved contact interface for dimer formation, which is absent from the enzymes described here.…”

Section: Resultsmentioning

confidence: 99%

“…This is consistent with the SEC-MALS results presented previously. Indeed, to the present date, the only members of the AKR superfamily which are known to be homodimers are aflatoxin dialdehyde reductase (AKR7A1), NAD(P)H dependent xylose reductase (AKR2B5), and the tyrosine auxotrophy suppressor protein (Kavanagh et al, 2003; Kozma et al, 2002; Obmolova et al, 2003). A similar dimerization interface using helices α5, α6, H2, and Loop-C is observed in all of these structures (figure S3).…”

Section: Resultsmentioning

confidence: 99%

Structural Characterization of L-Galactose Dehydrogenase: A Key Enzyme for Vitamin C Biosynthesis

Vargas

Leonardo

Pereira

et al. 2022

Preprint

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In plants, it is well-known that ascorbic acid (vitamin C) can be synthesized via multiple metabolic pathways but there is still much to be learnt concerning their integration and control mechanisms. Furthermore, the structural biology of the component enzymes has been poorly exploited. Here we describe the first crystal structure for an L-galactose dehydrogenase (SoGDH from spinach), from the D-mannose/L-galactose (Smirnoff Wheeler) pathway which converts L-galactose into L-galactono-1,4-lactone. The kinetic parameters for the enzyme are similar to those from its homologue from camu-camu, a super-accumulator of vitamin C found in the Peruvian amazon. Both enzymes are monomers in solution, have a pH optimum of 7 and their activity is largely unaffected by high concentrations of ascorbic acid, suggesting the absence of a feedback mechanism acting via GDH. Previous reports may have been influenced by changes of the pH of the reaction medium as a function of ascorbic acid concentration. The structure of SoGDH is dominated by a (β/α)8 barrel closely related to aldehyde-keto reductases (AKRs). The structure bound to NAD+ shows that the lack of Arg279 justifies its preference for NAD+ over NADP+, as employed by many AKRs. This favours the oxidation reaction which ultimately leads to ascorbic acid accumulation. When compared with other AKRs, residue substitutions at the C-terminal end of the barrel (Tyr185, Tyr61, Ser59 and Asp128) can be identified to be likely determinants of substrate specificity. The present work contributes towards a more comprehensive understanding of structure-function relationships in the enzymes involved in vitamin C synthesis.

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Crystal structure of the Escherichia coli Tas protein, an NADP(H)‐dependent aldo‐keto reductase

Cited by 8 publications

References 22 publications

Characterization of Two Novel Aldo–Keto Reductases from Arabidopsis: Expression Patterns, Broad Substrate Specificity, and an Open Active-Site Structure Suggest a Role in Toxicant Metabolism Following Stress

Characterization of Two Novel Aldo–Keto Reductases from Arabidopsis: Expression Patterns, Broad Substrate Specificity, and an Open Active-Site Structure Suggest a Role in Toxicant Metabolism Following Stress

The diversity of microbial aldo/keto reductases from Escherichia coli K12

Structural Characterization of L-Galactose Dehydrogenase: A Key Enzyme for Vitamin C Biosynthesis

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