3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

Wang, Yue; Li, Ping‐Yi; Zhang, Yi; Cao, Hai‐Yan; Wang, Yanjun; Li, Chunyang; Wang, Peng; Su, Hai-Nan; Chen, Yin; Chen, Xiu-Lan; Zhang, Yuzhong

doi:10.1016/j.jmb.2020.02.008

Cited by 7 publications

(12 citation statements)

References 45 publications

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“…30 The residues that make up the substrate pocket determine the physicochemical properties of the substrate, such as its charge, shape, and size. 9 By determining the substrate pocket of the enzyme and formulating effective transformation strategies, the enzyme's catalytic rate, specificity, and promiscuity can be optimized. 31 Zhou et al used the "polarity scanning" strategy to adjust the charge properties in the substrate pocket of alcohol dehydrogenase, and mutants with enhanced and inverted stereoselectivity were obtained.…”

Section: Resultsmentioning

confidence: 99%

“…In most enzymes, the substrate pocket is the core region to perform catalytic functions . The residues that make up the substrate pocket determine the physicochemical properties of the substrate, such as its charge, shape, and size . By determining the substrate pocket of the enzyme and formulating effective transformation strategies, the enzyme’s catalytic rate, specificity, and promiscuity can be optimized .…”

Section: Resultsmentioning

confidence: 99%

“…Previous reports have shown that some ALDHs have strong substrate specificity, which is due to the different charges and volumes of the substrate pockets in different types of ALDHs. For example, the substrate pocket of succinic semialdehyde dehydrogenase is positively charged to accommodate negatively charged succinic semialdehydes; the substrate pocket of betaine aldehyde dehydrogenase is negatively charged to accommodate positively charged betaine aldehydes; and 3,6-anhydro-α- l -galactose dehydrogenase has a large substrate pocket to allow the entry of 3,6-anhydro-α- l -galactose, while lactaldehyde dehydrogenase does not . Therefore, the substrate pocket determines the catalytic type of ALDHs, and modifying the substrate pocket has become one of the strategies to enhance the activity of ALDHs.…”

Section: Introductionmentioning

confidence: 99%

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Computer-Aided Semi-Rational Design to Enhance the Activity of l-Sorbosone Dehydrogenase from Gluconobacter oxidans WSH-004

Li,

Wang,

Huo

et al. 2024

J. Agric. Food Chem.

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The titer of the microbial fermentation products can be increased by enzyme engineering. L-Sorbosone dehydrogenase (SNDH) is a key enzyme in the production of 2-keto-L-gulonic acid (2-KLG), which is the precursor of vitamin C. Enhancing the activity of SNDH may have a positive impact on 2-KLG production. In this study, a computer-aided semirational design of SNDH was conducted. Based on the analysis of SNDH's substrate pocket and multiple sequence alignment, three modification strategies were established: (1) expanding the entrance of SNDH's substrate pocket, (2) engineering the residues within the substrate pocket, and (3) enhancing the electron transfer of SNDH. Finally, mutants S453A, L460V, and E471D were obtained, whose specific activity was increased by 20, 100, and 10%, respectively. In addition, the ability of Gluconobacter oxidans WSH-004 to synthesize 2-KLG was improved by eliminating H 2 O 2 . This study provides mutant enzymes and metabolic engineering strategies for the microbial-fermentation-based production of 2-KLG.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Computer-Aided Semi-Rational Design to Enhance the Activity of l-Sorbosone Dehydrogenase from Gluconobacter oxidans WSH-004

Li,

Wang,

Huo

et al. 2024

J. Agric. Food Chem.

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“…Therefore, the role of Cys-293 in the SCO3486 protein is expected to be important among the four catalytic residues. Moreover, recent studies on three-dimensional structures of AHG dehydrogenase revealed that Glu-259 and Cys-293 are important for its catalytic activity [ 28 ].…”

Section: Discussionmentioning

confidence: 99%

NADP⁺-Dependent Dehydrogenase SCO3486 and Cycloisomerase SCO3480: Key Enzymes for 3,6-Anhydro-L-Galactose Catabolism inStreptomyces coelicolorA3(2)

Tsevelkhorloo

Kim

Kang

et al. 2021

J. Microbiol. Biotechnol.

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Marine red algal cells contain high amounts of cellular carbohydrates and low amounts of lignin, and thus have gained attention as a sustainable next-generation biomass resource. Red algae-derived carbohydrates can replace fossil fuels, which are expected to be depleted in the near future, and can be converted into chemical feedstocks and bioenergy [1,2].Consisting mainly of carbohydrates that make up the majority of red algal cells, agar is a copolymer of the agarobiose unit (4-O-β-D-galactopyranosyl-3,6-anhydro-L-galactose) and the porphyrobiose unit (4-O-β-Dgalactopyranosyl-L-galactose-6-sulfate), linked by alpha-1,3 glycosidic bonds. The composition ratio of the two units varies depending on the species of red algae. Agar is called 'agarose' when agarobiose is the main component, and 'porphyran' when porphyrobiose is the main component [1,3].Agar has been widely used as a food, food additive, culturing medium, and support material for techniques like electrophoresis and chromatography [2]. Moreover, as the various biological activities of agar-derived oligosaccharides and agar decomposition products are discovered, the industrial use of agar is expected to expand [4]. Agarose, in nature, is mainly hydrolyzed by microbial beta-agarases into neoagarobiose (3,6-anhydro-Lgalactosyl-α-1,3-D-galactose), which is further hydrolyzed by neoagarooligosaccharide (NAOS) hydrolase into monomers D-galactose (D-Gal) and 3,6-anhydro-L-galactose (L-AHG) [5]. D-Gal is a valuable chemical feedstock that can be converted into bioenergy or other useful chemicals [4]. Additionally, L-AHG is a rare monosaccharide Agarose is a linear polysaccharide composed of D-galactose and 3,6-anhydro-L-galactose (AHG). It is a major component of the red algal cell wall and is gaining attention as an abundant marine biomass.However, the inability to ferment AHG is considered an obstacle in the large-scale use of agarose and could be addressed by understanding AHG catabolism in agarolytic microorganisms. Since AHG catabolism was uniquely confirmed in Vibrio sp. EJY3, a gram-negative marine bacterial species, we investigated AHG metabolism in Streptomyces coelicolor A3(2), an agarolytic gram-positive soil bacterium. Based on genomic data, the SCO3486 protein (492 amino acids) and the SCO3480 protein (361 amino acids) of S. coelicolor A3(2) showed identity with H2IFE7.1 (40% identity) encoding AHG dehydrogenase and H2IFX0.1 (42% identity) encoding 3,6-anhydro-L-galactonate cycloisomerase, respectively, which are involved in the initial catabolism of AHG in Vibrio sp. EJY3. Thin layer chromatography and mass spectrometry of the bioconversion products catalyzed by recombinant SCO3486 and SCO3480 proteins, revealed that SCO3486 is an AHG dehydrogenase that oxidizes AHG to 3,6-anhydro-L-galactonate, and SCO3480 is a 3,6-anhydro-L-galactonate cycloisomerase that converts 3,6-anhydro-L-galactonate to 2-keto-3-deoxygalactonate. SCO3486 showed maximum activity at pH 6.0 at 50°C, increased activity in the presence of iron ions, and activity against various a...

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“…The bioconversion of AHG is a bottleneck for red algae fermentation since AHG is a rare and untapped sugar. In recent years, researchers have discovered more of the AHG metabolic pathway and continue to develop related enzymes in this pathway to provide more options for metabolic engineering. − The proposed AHG pathway starts from converting AHG to AHGA through the oxidation of an aldehyde group . AHGA is then isomerized to form KDGal by AHGA cycloisomerase.…”

Section: Biotransformation Of Macroalgae Polysaccharidesmentioning

confidence: 99%

Recent Advances in Bioutilization of Marine Macroalgae Carbohydrates: Degradation, Metabolism, and Fermentation

Zheng

Yang

et al. 2022

J. Agric. Food Chem.

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Marine macroalgae are considered renewable natural resources due to their high carbohydrate content, which gives better utilization value in biorefineries and higher value conversion than firstand second-generation biomass. However, due to the diverse composition, complex structure, and rare metabolic pathways of macroalgae polysaccharides, their bioavailability needs to be improved. In recent years, enzymes and pathways related to the degradation and metabolism of macroalgae polysaccharides have been continuously developed, and new microbial fermentation platforms have emerged. Aiming at the bioutilization and transformation of macroalgae resources, this review describes the latest research results from the direction of green degradation, biorefining, and metabolic pathway design, including summarizing the the latest biorefining technology and the fermentation platform design of agarose, alginate, and other polysaccharides. This information will provide new research directions and solutions for the biotransformation and utilization of marine macroalgae.

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3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

Abstract: Please refer to published version for the most recent bibliographic citation information. If a published version is known of, the repository item page linked to above, will contain details on accessing it.

Cited by 7 publications

References 45 publications

Computer-Aided Semi-Rational Design to Enhance the Activity of l-Sorbosone Dehydrogenase from Gluconobacter oxidans WSH-004

Computer-Aided Semi-Rational Design to Enhance the Activity of l-Sorbosone Dehydrogenase from Gluconobacter oxidans WSH-004

NADP⁺-Dependent Dehydrogenase SCO3486 and Cycloisomerase SCO3480: Key Enzymes for 3,6-Anhydro-L-Galactose Catabolism inStreptomyces coelicolorA3(2)

Recent Advances in Bioutilization of Marine Macroalgae Carbohydrates: Degradation, Metabolism, and Fermentation

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3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

Abstract: Please refer to published version for the most recent bibliographic citation information. If a published version is known of, the repository item page linked to above, will contain details on accessing it.

Cited by 7 publications

References 45 publications

Computer-Aided Semi-Rational Design to Enhance the Activity of l-Sorbosone Dehydrogenase from Gluconobacter oxidans WSH-004

Computer-Aided Semi-Rational Design to Enhance the Activity of l-Sorbosone Dehydrogenase from Gluconobacter oxidans WSH-004

NADP+-Dependent Dehydrogenase SCO3486 and Cycloisomerase SCO3480: Key Enzymes for 3,6-Anhydro-L-Galactose Catabolism inStreptomyces coelicolorA3(2)

Recent Advances in Bioutilization of Marine Macroalgae Carbohydrates: Degradation, Metabolism, and Fermentation

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Product

Resources

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NADP⁺-Dependent Dehydrogenase SCO3486 and Cycloisomerase SCO3480: Key Enzymes for 3,6-Anhydro-L-Galactose Catabolism inStreptomyces coelicolorA3(2)