ArticleJournal of bacteriology1999
The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn(2+) flavoprotein.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- Mechanistic insights into redox activity and catalytic determinants of the haloarchaeal flavin-dependent oxidoreductasebioRxiv : the preprint server for biology · 2026Article
- Shotgun metagenomic mining reveals a new FAD-dependent D-lactate dehydrogenase in an isopod gut microbiome.Applied and environmental microbiology · 2025Article
- Lactate dehydrogenase D is a general dehydrogenase for D-2-hydroxyacids and is associated with D-lactic acidosis.Nature communications · 2023Article
- Aptamer-Based Diagnostic Systems for the Rapid Screening of TB at the Point-of-Care.Diagnostics (Basel, Switzerland) · 2021Review
- A D-lactate dehydrogenase from rice is involved in conferring tolerance to multiple abiotic stresses by maintaining cellular homeostasis.Scientific reports · 2020Article
- Enzymological characteristics of a novel archaeal dye-linked D-lactate dehydrogenase showing loose binding of FAD.Extremophiles : life under extreme conditions · 2018Article
- A Bacterial Multidomain NAD-Independent d-Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d-Lactate Oxidization.Journal of bacteriology · 2017Article
- Saccharomyces cerevisiae Forms D-2-Hydroxyglutarate and Couples Its Degradation to D-Lactate Formation via a Cytosolic Transhydrogenase.The Journal of biological chemistry · 2016Article
- Utilization of D-Lactate as an Energy Source Supports the Growth of Gluconobacter oxydans.Applied and environmental microbiology · 2015Article
- Tandem prenyltransferases catalyze isoprenoid elongation and complexity generation in biosynthesis of quinolone alkaloids.Journal of the American Chemical Society · 2015Article
- The primary pathway for lactate oxidation in Desulfovibrio vulgaris.Frontiers in microbiology · 2015Article
- Identification of key components in the energy metabolism of the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus by transcriptome analyses.Frontiers in microbiology · 2014Article
- Crystallization and preliminary X-ray analysis of a dye-linked D-lactate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Genetics and molecular biology of the electron flow for sulfate respiration in desulfovibrio.Frontiers in microbiology · 2011Article
- Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and beta-oxidation pathways.The Journal of biological chemistry · 2009Article
- Evolutionary history of D-lactate dehydrogenases: a phylogenomic perspective on functional diversity in the FAD binding oxidoreductase/transferase type 4 family.Journal of molecular evolution · 2009Article
- Identification of a dehydrogenase acting on D-2-hydroxyglutarate.The Biochemical journal · 2004Article
- Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus.Archaea (Vancouver, B.C.) · 2002Article
- D-Lactate transport and metabolism in rat liver mitochondria.The Biochemical journal · 2002Article
- H(2)O(2)-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus.Journal of bacteriology · 2001Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Archaeoglobus fulgidus, a hyperthermophilic, archaeal sulfate reducer, is one of the few organisms that can utilize D-lactate as a sole source for both carbon and electrons. The A. fulgidus open reading frame, AF0394, which is predicted to encode a D-(-)-lactate dehydrogenase (Dld), was cloned, and its product was expressed in Escherichia coli as a fusion with the maltose binding protein (MBP). The 90-kDa MBP-Dld fusion protein was more efficiently expressed in E. coli when coexpressed with the E. coli dnaY gene, encoding the arginyl tRNA for the codons AGA and AGG. When cleaved from the fusion protein by treatment with factor Xa, the recombinant Dld (rDld) has an apparent molecular mass of 50 kDa, similar to that of the native A. fulgidus Dld enzyme. Both the purified MBP-Dld fusion protein and its rDld cleavage fragment have lactate dehydrogenase activities specific for D-lactate, are stable at 80 degrees C, and retain activity after exposure to oxygen. The flavin cofactor FAD, which binds rDld apoprotein with a 1:1 stoichiometry, is essential for activity.
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