4do7: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/FCNLN_BURM1 FCNLN_BURM1] L-fucono-1,5-lactonase involved in an L-fucose degradation pathway (PubMed:23214453). Catalyzes the hydrolysis of L-fucono-1,5-lactone to L-fuconate (PubMed:23214453). L-fucono-1,5-lactone is the best substrate, but the enzyme can also hydrolyze L-fucono-1,4-lactone, L-galactono-1,4-lactone D-arabinono-1,4-lactone and L-xylono-1,4-lactone (PubMed:23214453).<ref>PMID:23214453</ref> | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Latest revision as of 11:18, 9 October 2024
Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2
Structural highlights
FunctionFCNLN_BURM1 L-fucono-1,5-lactonase involved in an L-fucose degradation pathway (PubMed:23214453). Catalyzes the hydrolysis of L-fucono-1,5-lactone to L-fuconate (PubMed:23214453). L-fucono-1,5-lactone is the best substrate, but the enzyme can also hydrolyze L-fucono-1,4-lactone, L-galactono-1,4-lactone D-arabinono-1,4-lactone and L-xylono-1,4-lactone (PubMed:23214453).[1] References
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