L-fucose isomerase
| L-fucose isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.3.1.25 | ||||||||
| CAS number | 60063-83-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
| L-fucose isomerase, first N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 l-fucose isomerase from escherichia coli | |||||||||
| Identifiers | |||||||||
| Symbol | Fucose_iso_N1 | ||||||||
| Pfam | PF07881 | ||||||||
| InterPro | IPR012888 | ||||||||
| SCOP | 1fui | ||||||||
| SUPERFAMILY | 1fui | ||||||||
| |||||||||
| L-fucose isomerase, second N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
l-fucose isomerase from escherichia coli | |||||||||
| Identifiers | |||||||||
| Symbol | Fucose_iso_N2 | ||||||||
| Pfam | PF07882 | ||||||||
| InterPro | IPR012889 | ||||||||
| SCOP | 1fui | ||||||||
| SUPERFAMILY | 1fui | ||||||||
| |||||||||
| L-fucose isomerase, C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
l-fucose isomerase from escherichia coli | |||||||||
| Identifiers | |||||||||
| Symbol | Fucose_iso_C | ||||||||
| Pfam | PF02952 | ||||||||
| Pfam clan | CL0393 | ||||||||
| InterPro | IPR015888 | ||||||||
| SCOP | 1fui | ||||||||
| SUPERFAMILY | 1fui | ||||||||
| |||||||||
In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reaction
- L-fucose L-fuculose
Hence, this enzyme has one substrate, L-fucose, and one product, L-fuculose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose metabolism.
The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The structure was determined by X-ray crystallography at 2.5 Angstrom resolution.[1] Each subunit of the hexameric enzyme is wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues.[1]
References
Further reading
- Lu Z, Lin EC (1989). "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation". Nucleic. Acids. Res. 17 (12): 4883–4. doi:10.1093/nar/17.12.4883. PMC 318048
. PMID 2664711.
This article incorporates text from the public domain Pfam and InterPro IPR015888
This article incorporates text from the public domain Pfam and InterPro IPR012889
This article incorporates text from the public domain Pfam and InterPro IPR012888