ArticleBiochemistry2009
Structural and functional studies of QdtC: an N-acetyltransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-glucose.
Article in Biochemistry, 2009. 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, 25 citations in OpenAlex.
- Mechanistic plasticity in ApmA enables aminoglycoside promiscuity for resistance.Nature chemical biology · 2024Article
- Structural and functional insights into δ-poly-L-ornithine polymer biosynthesis from Acinetobacter baumannii.Communications biology · 2023Article
- Investigation of the enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-d-glucuronic acid in Psychrobacter cryohalolentis K5Protein science : a publication of the Protein Society · 2023Article
- Structure and function of an N-acetyltransferase from the human pathogen Acinetobacter baumannii isolate BAL_212.Proteins · 2022Article
- Biochemical investigation of an N-acetyltransferase from Helicobacter pullorum.Protein science : a publication of the Protein Society · 2021Article
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- The rare sugarThe Journal of biological chemistry · 2017Article
- Structural and Functional Investigation of FdhC from Acinetobacter nosocomialis: A Sugar N-Acyltransferase Belonging to the GNAT Superfamily.Biochemistry · 2016Article
- Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.Insect biochemistry and molecular biology · 2015Article
- Article
- Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.Biochemistry · 2014Article
- Structure of soybean serine acetyltransferase and formation of the cysteine regulatory complex as a molecular chaperone.The Journal of biological chemistry · 2013Article
- Structural and biochemical characterization of a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans.Biochemistry · 2013Article
- Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine.The Journal of biological chemistry · 2013Article
- Structure of a sugar N-formyltransferase from Campylobacter jejuni.Biochemistry · 2013Article
- The structural biology of enzymes involved in natural product glycosylation.Natural product reports · 2012Review
- Catalytic mechanism of perosamine N-acetyltransferase revealed by high-resolution X-ray crystallographic studies and kinetic analyses.Biochemistry · 2012Article
- The s-layer glycome-adding to the sugar coat of bacteria.International journal of microbiology · 2011Article
- Biosynthetic enzymes of unusual microbial sugars.Current opinion in structural biology · 2010Review
- Molecular structure of WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid .Biochemistry · 2010Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
3-Acetamido-3,6-dideoxy-alpha-D-glucose or Quip3NAc is an unusual dideoxy sugar found in the O-antigens of various Gram-negative bacteria and in the S-layer glycoprotein glycans of some Gram-positive bacteria. It is produced in these organisms as a dTDP-linked sugar, with five enzymes ultimately required for its biosynthesis. The focus of this investigation is on the enzyme QdtC, a CoA-dependent N-acetyltransferase that catalyzes the last step in the Quip3NAc biosynthetic pathway. For this analysis, three crystal structures were determined: the wild-type enzyme in the presence of acetyl-CoA and two ternary complexes of the enzyme with CoA and either dTDP-D-Quip3N or dTDP-3-amino-3,6-didexoy-alpha-D-galactose (dTDP-D-Fucp3N). Each subunit of the trimeric enzyme is dominated by a left-handed beta-helix motif with 11 turns. The three active sites are located at the subunit-subunit interfaces, and the two dTDP-sugar ligands employed in this study bind to the protein in nearly identical manners. Those residues responsible for anchoring the hexose moieties of the dTDP-sugars to the protein include Glu 141, Asn 159, and Asp 160 from one subunit and His 134 from another subunit. To probe the roles of various amino acid residues in the catalytic mechanism of the enzyme, 10 site-directed mutant proteins were constructed and their kinetic parameters measured. On the basis of these data, a catalytic mechanism is proposed for QdtC in which the acetylation of the sugar amino group does not require a catalytic base provided by the protein. Rather, the sulfur of CoA functions as the ultimate proton acceptor.
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