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Literature summary extracted from
- Structural and functional analysis of fucose-processing enzymes from Streptococcus pneumoniae (2014), J. Mol. Biol., 426, 1469-1482 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.3.1.25 | medicine | the Streptococcus pneumoniae fucose-processing pathway has a nonmetabolic role in the interaction of this bacterium with its human host | Streptococcus pneumoniae |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.25 | Streptococcus pneumoniae | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.25 | FcsI | - |
Streptococcus pneumoniae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.3.1.25 | physiological function | fucose-processing enzymes fucose isomerase (FcsI), fuculose kinase (FcsK), and fuculose-1-phosphate aldolase (FcsA) act in a sequential manner to ultimately produce dihydroxyacetone phosphate. Fuculose-1-phosphate appears to act as an inducing molecule for activation of the fucose operon. The Streptococcus pneumoniae fucose-processing pathway has a nonmetabolic role in the interaction of this bacterium with its human host | Streptococcus pneumoniae |
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Release 2023.1 (January 2023)
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