An Extended β7α7 Substrate-Binding Loop Is Essential for Efficient Catalysis by 3-Deoxy-d-manno-Octulosonate 8-Phosphate Synthase
Author:
Affiliation:
1. Biomolecular Interaction Centre and Department of Chemistry, University of Canterbury, Christchurch, New Zealand
2. The Riddet Institute and The Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi201231e
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2. Antibacterial and anti-inflammatory agents that target endotoxin
3. The Correct Phylogenetic Relationship of KdsA (3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase) with One of Two Independently Evolved Classes of AroA (3-Deoxy-D-arabino-heptulosonate 7-Phosphate Synthase)
4. Substrate Ambiguity of 3-Deoxy- d - manno -Octulosonate 8-Phosphate Synthase from Neisseria gonorrhoeae in the Context of Its Membership in a Protein Family Containing a Subset of 3-Deoxy- d - arabino -Heptulosonate 7-Phosphate Synthases
5. Aquifex aeolicus 3-Deoxy-d-manno-2-Octulosonic Acid 8-Phosphate Synthase: A New Class of KDO 8-P Synthase?
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3. Structure of 2-keto-3-deoxy-D-manno-octulosonate-8-phosphate synthase fromPseudomonas aeruginosa;Acta Crystallographica Section F Structural Biology and Crystallization Communications;2013-09-28
4. Examining the Role of Intersubunit Contacts in Catalysis by 3-Deoxy-d-manno-octulosonate 8-Phosphate Synthase;Biochemistry;2013-06-26
5. Functional roles of H98 and W99 and β2α2 loop dynamics in the α-l -arabinofuranosidase from Thermobacillus xylanilyticus;The FEBS Journal;2012-08-31
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