L-fuculose-phosphate aldolase
| L-fuculose-phosphate aldolase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.1.2.17 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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 | ||||||||
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In enzymology, a L-fuculose-phosphate aldolase (EC 4.1.2.17) is an enzyme that catalyzes the chemical reaction
- L-fuculose-1-phosphate
glycerone phosphate + (S)-lactaldehyde
Hence, this enzyme has one substrate, L-fuculose-1-phosphate, and two products, glycerone phosphate and (S)-lactaldehyde.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming). Other names in common use include L-fuculose 1-phosphate aldolase, fuculose aldolase, and L-fuculose-1-phosphate lactaldehyde-lyase. This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1DZU, 1DZV, 1DZW, 1DZX, 1DZY, 1DZZ, 1E46, 1E47, 1E48, 1E49, 1E4A, 1E4B, 1E4C, 1FUA, 2FK5, 2FLF, 2FUA, 2OPI, 3FUA, and 4FUA.
See also
References
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