ArticleProtein science : a publication of the Protein Society2007
Molecular architecture of DesV from Streptomyces venezuelae: a PLP-dependent transaminase involved in the biosynthesis of the unusual sugar desosamine.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 36 citations in OpenAlex.
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- Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.Biochemistry · 2017Article
- Structural investigation on WlaRG from Campylobacter jejuni: A sugar aminotransferase.Protein science : a publication of the Protein Society · 2017Article
- Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases.ACS chemical biology · 2015Article
- Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis.Proteins · 2015Article
- The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.The Journal of biological chemistry · 2013Article
- The structural biology of enzymes involved in natural product glycosylation.Natural product reports · 2012Review
- Mechanisms and structures of vitamin B(6)-dependent enzymes involved in deoxy sugar biosynthesis.Biochimica et biophysica acta · 2011Review
- Biosynthetic enzymes of unusual microbial sugars.Current opinion in structural biology · 2010Review
- Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly.Biochemistry · 2010Article
- Purification, crystallization and preliminary X-ray analysis of NtdA, a putative pyridoxal phosphate-dependent aminotransferase from Bacillus subtilis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Structural analysis of QdtB, an aminotransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-glucose.Biochemistry · 2009Article
- Structure and mutagenic conversion of E1 dehydrase: at the crossroads of dehydration, amino transfer, and epimerization.Biochemistry · 2008Article
- Increasing carbohydrate diversity via amine oxidation: aminosugar, hydroxyaminosugar, nitrososugar, and nitrosugar biosynthesis in bacteria.Current opinion in chemical biology · 2008Review
- Natural-product sugar biosynthesis and enzymatic glycodiversification.Angewandte Chemie (International ed. in English) · 2008Review
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3 authors at 1 institution in 1 country.
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Abstract
Desosamine is a 3-(dimethylamino)-3,4,6-trideoxyhexose found in certain macrolide antibiotics such as the commonly prescribed erythromycin. Six enzymes are required for its biosynthesis in Streptomyces venezuelae. The focus of this article is DesV, which catalyzes the PLP-dependent replacement of a 3-keto group with an amino functionality in the fifth step of the pathway. For this study the three-dimensional structures of both the internal aldimine and the ketimine intermediate with glutamate were determined to 2.05 A resolution. DesV is a homodimer with each subunit containing 12 alpha-helical regions and 12 beta-strands that together form three layers of sheet. The structure of the internal aldimine demonstrates that the PLP-cofactor is held in place by residues contributed from both subunits (Asp 164 and Gln 167 from Subunit I and Tyr 221 and Asn 235 from Subunit II). When the ketimine intermediate is present in the active site, the loop defined by Gln 225 to Ser 228 from Subunit II closes down upon the active site. The structure of DesV is similar to another sugar-modifying enzyme referred to as PseC. This enzyme is involved in the biosynthesis of pseudaminic acid, which is a sialic acid-like nonulosonate found in the flagellin of Helicobacter pylori. In the case of PseC, however, the amino group is transferred to the C-4 rather than the C-3 position. Details concerning the structural analysis of DesV and a comparison of its molecular architecture to that of PseC are presented.
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