Journal: The Journal of Biological Chemistry

Article Title: Biochemical and structural basis of sialic acid utilization by gut microbes

doi: 10.1016/j.jbc.2023.102989

Figure Lengend Snippet: List of functionally characterized sialic acid enzymes and transporters from gut bacteria

Article Snippet: Both ATCC 29149 and ATCC 35913 strains R. gnavus strains were able to grow on 2,7-anyhydro-Neu5Ac, the IT-sialidase transglycosylation product, as a sole carbon source ( ).

Techniques: Bacteria, Membrane, Labeling

Journal: The Journal of Biological Chemistry

Article Title: Biochemical and structural basis of sialic acid utilization by gut microbes

doi: 10.1016/j.jbc.2023.102989

Figure Lengend Snippet: Structural characteristics of sialic acid catabolic enzymes from gut bacteria. A , crystal structure of B. thetaiotaomicron VPI-5482 sialidase with catalytic domain in teal and proposed CBM40 domain in wheat (PDB 4BBW ). The active site is indicated by a red sphere. Close-up of the active site shows the catalytic residues in orange and the arginine triad in green. In gray is the aligned crystal structure of S. pneumoniae NanA (PDB 2YA5 ) with sialic acid bound in yellow. B , composite structure of R. gnavus IT-sialidase Rg NanH. The catalytic domain in complex with 2,7-anhydro-Neu5Ac and inserted domain, pink and light blue , respectively (PDB 4X4A ), and in green the CBM40 domain in complex with 2,3-sialyllactose (PDB 6ER3 ). The residues responsible for reaction specificity are highlighted with a yellow surface. The VPI-5482 sialidase is aligned in teal for comparison. C , 9-O-acetylesterase from P. vulgatus (PDB: 7PZG ). The SGNH motif is highlighted with a pink surface and the canonical catalytic in orange in the active-site close-up. PDB, Protein Data Bank.

Article Snippet: Both ATCC 29149 and ATCC 35913 strains R. gnavus strains were able to grow on 2,7-anyhydro-Neu5Ac, the IT-sialidase transglycosylation product, as a sole carbon source ( ).

Techniques: Bacteria, Comparison

Journal: The Journal of Biological Chemistry

Article Title: Biochemical and structural basis of sialic acid utilization by gut microbes

doi: 10.1016/j.jbc.2023.102989

Figure Lengend Snippet: Schematic representation of the sialic acid metabolic pathways identified in gut bacteria. A , E. coli Neu5Ac metabolism. B , B. fragilis Neu5Ac metabolism. C , R. gnavus 2,7-anhydro-Neu5Ac metabolism. Difference in the pathways are highlighted: orange , 2,7-anhydro-Neu5Ac metabolic pathway; green , “ E. coli ” Neu5Ac metabolic pathway; blue , B. fragilis Neu5Ac metabolic pathway.

Article Snippet: Both ATCC 29149 and ATCC 35913 strains R. gnavus strains were able to grow on 2,7-anyhydro-Neu5Ac, the IT-sialidase transglycosylation product, as a sole carbon source ( ).

Techniques: Bacteria

Journal: The Journal of Biological Chemistry

Article Title: Biochemical and structural basis of sialic acid utilization by gut microbes

doi: 10.1016/j.jbc.2023.102989

Figure Lengend Snippet: Structural characteristics of 2,7-anhydro-Neu-5Ac metabolic enzymes. Once transported inside R. gnavus ATCC 29149 cells ( A ) Rg NanOx converts 2,7-anhydro-Neu5Ac into Neu5Ac with the aid of an NAD cofactor. The NAD cofactor and a bound citrate molecule are shown in yellow and green , respectively (PDB 6Z3C). B , Neu5Ac is subsequently converted to ManNAc and pyruvate by Rg NanA. Neu5Ac in its open-chain ketone form is shown bound in the active site with catalytic residues in green (PDB 6RD1). For clarity, the surface representation has been omitted from the active site due to its buried nature. PDB, Protein Data Bank.

Article Snippet: Both ATCC 29149 and ATCC 35913 strains R. gnavus strains were able to grow on 2,7-anyhydro-Neu5Ac, the IT-sialidase transglycosylation product, as a sole carbon source ( ).

Techniques: