ArticleThe Journal of biological chemistry2014
Structure-based conversion of the coenzyme requirement of a short-chain dehydrogenase/reductase involved in bacterial alginate metabolism.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- A specific tripartite tricarboxylate transporter is involved in alginate utilization byApplied and environmental microbiology · 2026Article
- Homologous relationship between FabG involved in fatty acid biosynthesis and SDR on chromosome II in the multi-chromosome pathogen Vibrio anguillarum.Scientific reports · 2025Article
- Substrate size-dependent conformational changes of bacterial pectin-binding protein crucial for chemotaxis and assimilation.Scientific reports · 2022Article
- Rossmann-toolbox: a deep learning-based protocol for the prediction and design of cofactor specificity in Rossmann fold proteins.Briefings in bioinformatics · 2022Article
- 4-Deoxy-l-Molecules (Basel, Switzerland) · 2022Review
- Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022Article
- Toward Understanding the Alginate Catabolism inFrontiers in bioengineering and biotechnology · 2022Article
- An oxidative metabolic pathway of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEHU) from alginate in an alginate-assimilating bacterium.Communications biology · 2021Article
- Stromal NADH supplied by PHOSPHOGLYCERATE DEHYDROGENASE3 is crucial for photosynthetic performance.Plant physiology · 2021Article
- Dietary polyvinyl alcohol and alginate nanofibers ameliorate hyperglycemia by reducing insulin and glucose-metabolizing enzyme levels in rats with streptozotocin-induced diabetes.Veterinary world · 2021Article
- Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacteriumPeerJ · 2021Article
- Short-Chain Dehydrogenase NcmD Is Responsible for the C-10 Oxidation of Nocamycin F in Nocamycin Biosynthesis.Frontiers in microbiology · 2020Article
- Uncovering the reactive nature of 4-deoxy-L-erythro-5-hexoseulose uronate for the utilization of alginate, a promising marine biopolymer.Scientific reports · 2019Article
- Functional identification of alginate lyase from the brown alga Saccharina japonica.Scientific reports · 2019Article
- Substrate scope of a dehydrogenase from Sphingomonas species A1 and its potential application in the synthesis of rare sugars and sugar derivatives.Microbial biotechnology · 2018Article
- Identification of 4-Deoxy-L-Etychro-Hexoseulose Uronic Acid Reductases in an Alginolytic Bacterium Vibrio splendidus and their Uses for L-Lactate Production in an Escherichia coli Cell-Free System.Marine biotechnology (New York, N.Y.) · 2018Article
- Redox cofactor engineering in industrial microorganisms: strategies, recent applications and future directions.Journal of industrial microbiology & biotechnology · 2018Review
- Protein Engineering for Nicotinamide Coenzyme Specificity in Oxidoreductases: Attempts and Challenges.Frontiers in microbiology · 2018Review
- Protein engineering of oxidoreductases utilizing nicotinamide-based coenzymes, with applications in synthetic biology.Synthetic and systems biotechnology · 2017Review
- Crucial role of 4-deoxy-L-erythro-5-hexoseulose uronate reductase for alginate utilization revealed by adaptive evolution in engineered Saccharomyces cerevisiae.Scientific reports · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The alginate-assimilating bacterium, Sphingomonas sp. strain A1, degrades the polysaccharides to monosaccharides through four alginate lyase reactions. The resultant monosaccharide, which is nonenzymatically converted to 4-deoxy-L-erythro-5-hexoseulose uronate (DEH), is further metabolized to 2-keto-3-deoxy-D-gluconate by NADPH-dependent reductase A1-R in the short-chain dehydrogenase/reductase (SDR) family. A1-R-deficient cells produced another DEH reductase, designated A1-R', with a preference for NADH. Here, we show the identification of a novel NADH-dependent DEH reductase A1-R' in strain A1, structural determination of A1-R' by x-ray crystallography, and structure-based conversion of a coenzyme requirement in SDR enzymes, A1-R and A1-R'. A1-R' was purified from strain A1 cells and enzymatically characterized. Except for the coenzyme requirement, there was no significant difference in enzyme characteristics between A1-R and A1-R'. Crystal structures of A1-R' and A1-R'·NAD(+) complex were determined at 1.8 and 2.7 Å resolutions, respectively. Because of a 64% sequence identity, overall structures of A1-R' and A1-R were similar, although a difference in the coenzyme-binding site (particularly the nucleoside ribose 2' region) was observed. Distinct from A1-R, A1-R' included a negatively charged, shallower binding site. These differences were caused by amino acid residues on the two loops around the site. The A1-R' mutant with the two A1-R-typed loops maintained potent enzyme activity with specificity for NADPH rather than NADH, demonstrating that the two loops determine the coenzyme requirement, and loop exchange is a promising method for conversion of coenzyme requirement in the SDR family.
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