ArticleChemistry & biology2009
Alternative epimerization in C(7)N-aminocyclitol biosynthesis is catalyzed by ValD, a large protein of the vicinal oxygen chelate superfamily.
Article in Chemistry & biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- NonglycosidicSynthetic and systems biotechnology · 2025Article
- Metabolic engineering of a methyltransferase for production of drug precursors demecycline and demeclocycline inSynthetic and systems biotechnology · 2020Article
- Reliable Target Prediction of Bioactive Molecules Based on Chemical Similarity Without Employing Statistical Methods.Frontiers in pharmacology · 2019Article
- Biosynthesis and Metabolic Engineering of Pseudo-oligosaccharides.Emerging topics in life sciences · 2018Article
- Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to several distinct cyclic products.Journal of the American Chemical Society · 2012Article
- Genomic and transcriptomic insights into the thermo-regulated biosynthesis of validamycin in Streptomyces hygroscopicus 5008.BMC genomics · 2012Article
- Structural and functional analysis of validoxylamine A 7'-phosphate synthase ValL involved in validamycin A biosynthesis.PloS one · 2012Article
- Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis.Journal of the American Chemical Society · 2011Article
- Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Current opinion in structural biology · 2011Review
- Nucleotidylation of unsaturated carbasugar in validamycin biosynthesis.Organic & biomolecular chemistry · 2011Article
- Enhancement of the diversity of polyoxins by a thymine-7-hydroxylase homolog outside the polyoxin biosynthesis gene cluster.Applied and environmental microbiology · 2010Article
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6 authors.
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Abstract
Gene valD, encodes a large vicinal oxygen chelate (VOC) superfamily protein, has been identified in the validamycin biosynthetic gene cluster. Inactivation of valD significantly reduced validamycin A production, which was fully restored with the full-length valD and partially restored with either N-terminal or C-terminal half by complementation. Heterologously expressed ValD catalyzed the epimerization of 2-epi-5-epi-valiolone to 5-epi-valiolone. This metalloenzyme is a homodimer with a metal ion-binding ratio of 0.73 mol/mole protein toward Fe(2+), Mn(2+), Ni(2+), and Zn(2+). Individual and combined site-directed mutations of eight putative active site residues revealed that the N-terminal H44/E107 and the C-terminal H315/E366 are more critical for the activity than the internal H130, E183, H229, and E291. Our data have established ValD as one of the largest proteins of the VOC superfamily, catalyzing an alternative epimerization for C(7)N-aminocyclitol biosynthesis.
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