Structural and kinetic characterization of a maize aldose reductase

Sousa, S. M. de; Rosselli, Luciana Kauer; Kiyota, Eduardo; Silva, Júlio César da; Souza, Gustavo H.M.F.; Peroni, L; Stach-Machado, Dagmar Ruth; Eberlin, Marcos N.; Souza, Anete Pereira de; Koch, Karen E.; Arruda, Paulo; Torriani, Íris L.; Yunes, José Andrés

doi:10.1016/j.plaphy.2008.10.009

Cited by 17 publications

(14 citation statements)

References 32 publications

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“…20) Three loop structures (loops A, B, and C) adjacent to the (/) 8 -barrel are required for RC substrate specificity. 20) In higher plants, several enzymes have been reported to reduce sugar-derived RCs: AKR4C1 (barley), 23) AKR4C7 (maize), 24) AKR4C12 (aloe), 25) AKR4C14 (Indian rice), 26) OsAKR1 (Japonica rice), 27) and AKR4C8 and AKR4C9 (Arabidopsis). 1) All of these belong to the AKR4C subfamily.…”

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confidence: 99%

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]

Saito

Shimakawa

Nishi

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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In Arabidopsis thaliana, the aldo-keto reductase (AKR) family includes four enzymes (The AKR4C subfamily: AKR4C8, AKR4C9, AKR4C10, and AKR4C11). AKR4C8 and AKR4C9 might detoxify sugar-derived reactive carbonyls (RCs). We analyzed AKR4C10 and AKR4C11, and compared the enzymatic functions of the four enzymes. Modeling of protein structures based on the known structure of AKR4C9 found an (α/β)8-barrel motif in all four enzymes. Loop structures (A, B, and C) which determine substrate specificity, differed among the four. Both AKR4C10 and AKR4C11 reduced methylglyoxal. AKR4C10 reduced triose phosphates, dihydroxyacetone phosphate (DHAP), and glyceraldehydes 3-phosphate (GAP), the most efficiently of all the AKR4Cs. Acrolein, a lipid-derived RC, inactivated the four enzymes to different degrees. Expression of the AKR4C genes was induced under high-[CO2] and high light, when photosynthesis was enhanced and photosynthates accumulated in the cells. These results suggest that the AKR4C subfamily contributes to the detoxification of sugar-derived RCs in plants.

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confidence: 99%

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]

Saito

Shimakawa

Nishi

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…Recombinant AKR4C7 (UNIPROT ID: A2T1W7) fused to an Nterminal His-tag was overexpressed in Escherichia coli BL21(DE3), purified by metal-affinity and anion-exchange chromatographies [10], and crystallized by vapor diffusion as described by Kiyota and co-workers [11]. The AKR4C7$NADP þ complex was co-crystallized in a condition similar to that of the apoenzyme (0.1 M Tris-HCl, pH, 6.0, 22% m/v PEG4000 and 0.1 M sodium acetate) preincubating AKR4C7 at 9 mg/ml with 10 mM NADP þ .…”

Section: Protein Overexpression Purification and Crystallizationmentioning

confidence: 99%

“…Since the only apo structure of a plant AKR available thus far (AKR4C1) shows wellordered Loops A and C, further studies are required to determine whether substrate-induced structural change is a specific feature of AKR4C7 loops or shared with other plant AKRs such as AKR4C8 and AKR4C9. Although the closest relatives of the AKR4C subfamily in mammals are members of the AKR1 family, which include aldose reductases, the AKR4C enzymes are poorly active or even inactive with glucose and xylose [7,9,10]. We thus postulated that a molecular change to the active site could be responsible for impairment of the xylose/glucose reductase activity in AKR4C subfamily members.…”

Section: Substrate Binding Is Likely Required To Stabilize Loop B In mentioning

confidence: 99%

“…Functional and structural comparisons between the human aldose reductase AKR1B1 and the plant AKR4C subfamily members AKR4C7, AKR4C8 and AKR4C9. (A) A summary of affinity parameters for cofactor-and aldose-binding from literature: a [23,26], b [7], c [10]. (B, C and D) Surface topography of the AKR active sites determined using CASTp [27].…”

Section: Transparency Documentmentioning

confidence: 99%

“…However, in vitro studies show that these enzymes are poorly active or even inactive with glucose [7,9,10]. Although the structural basis for the substrate preferences of some AKR4C enzymes is known [6,7], the molecular adaptations that impair their function on osmoregulatory-relevant substrates, such as glucose, remain elusive.…”

Section: Introductionmentioning

confidence: 99%

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A comparative structural analysis reveals distinctive features of co-factor binding and substrate specificity in plant aldo-keto reductases

Giuseppe

Santos

Sousa

et al. 2016

Biochemical and Biophysical Research Communications

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Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops. However, these AKR4Cs show little to no activity with previously-envisioned sugar substrates. We hypothesized a structural basis for the distinctive cofactor binding and substrate specificity of these plant enzymes. To test this, we solved the crystal structure of a novel AKR4C subfamily member, the AKR4C7 from maize, in the apo form and in complex with NADP(+). The binary complex revealed an intermediate state of cofactor binding that preceded closure of Loop B, and also indicated that conformational changes upon substrate binding are required to induce a catalytically-favorable conformation of the active-site pocket. Comparative structural analyses of homologues (AKR1B1, AKR4C8 and AKR4C9) showed that evolutionary redesign of plant AKR4Cs weakened interactions that stabilize the closed conformation of Loop B. This in turn decreased cofactor affinity and altered configuration of the substrate-binding site. We propose that these structural modifications contribute to impairment of sugar reductase activity in favor of other substrates in the plant AKR4C subgroup, and that catalysis involves a three-step process relevant to other AKRs.

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Versatile roles of sorbitol in higher plants: luxury resource, effective defender or something else?

Dvořáková

Hamet

Konrádová

et al. 2022

Planta

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Structural and kinetic characterization of a maize aldose reductase

Cited by 17 publications

References 32 publications

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]

A comparative structural analysis reveals distinctive features of co-factor binding and substrate specificity in plant aldo-keto reductases

Versatile roles of sorbitol in higher plants: luxury resource, effective defender or something else?

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Structural and kinetic characterization of a maize aldose reductase

Cited by 17 publications

References 32 publications

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO2]

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO2]

A comparative structural analysis reveals distinctive features of co-factor binding and substrate specificity in plant aldo-keto reductases

Versatile roles of sorbitol in higher plants: luxury resource, effective defender or something else?

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Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]

Functional Analysis of the AKR4C Subfamily ofArabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]