ArticleThe Journal of biological chemistry2013
The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Review
- Impact of activation of neotrehalosadiamine/kanosamine biosynthetic pathway on the metabolism ofJournal of bacteriology · 2021Article
- Wobble Editing ofFrontiers in chemistry · 2021Article
- Biocatalytic Production of Amino Carbohydrates through Oxidoreductase and Transaminase Cascades.ChemSusChem · 2019Article
- Overview of the Antimicrobial Compounds Produced by Members of theFrontiers in microbiology · 2019Review
- Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement.Microbial biotechnology · 2018Article
- Structures of KdnB and KdnA from Shewanella oneidensis: Key Enzymes in the Formation of 8-Amino-3,8-Dideoxy-d-Manno-Octulosonic Acid.Biochemistry · 2016Article
- Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases.ACS chemical biology · 2015Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
NtdA from Bacillus subtilis is a sugar aminotransferase that catalyzes the pyridoxal phosphate-dependent equatorial transamination of 3-oxo-α-D-glucose 6-phosphate to form α-D-kanosamine 6-phosphate. The crystal structure of NtdA shows that NtdA shares the common aspartate aminotransferase fold (Type 1) with residues from both monomers forming the active site. The crystal structures of NtdA alone, co-crystallized with the product α-D-kanosamine 6-phosphate, and incubated with the amine donor glutamate reveal three key structures in the mechanistic pathway of NtdA. The structure of NtdA alone reveals the internal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys-247. The addition of glutamate results in formation of pyridoxamine phosphate. Co-crystallization with kanosamine 6-phosphate results in the formation of the external aldimine. Only α-D-kanosamine 6-phosphate is observed in the active site of NtdA, not the β-anomer. A comparison of the structure and sequence of NtdA with other sugar aminotransferases enables us to propose that the VIβ family of aminotransferases should be divided into subfamilies based on the catalytic lysine motif.
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