Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.1 Carboxylic-ester hydrolases
ID:3.1.1.15
Description:L-arabinonolactonase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.1.15
BRENDA Enzyme Link: BRENDA 3.1.1.15
KEGG Enzyme Link: KEGG3.1.1.15
BioCyc Enzyme Link: BioCyc 3.1.1.15
ExPASy Enzyme Link: ExPASy3.1.1.15
EC2PDB Enzyme Link: EC2PDB 3.1.1.15
ExplorEnz Enzyme Link: ExplorEnz 3.1.1.15
PRIAM enzyme-specific profiles Link: PRIAM 3.1.1.15
IntEnz Enzyme Link: IntEnz 3.1.1.15
MEDLINE Enzyme Link: MEDLINE 3.1.1.15
MSA:

3.1.1.15;

Phylogenetic Tree:

3.1.1.15;

Uniprot:
M-CSA:
RHEA:16217 H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[OH2;+0:6]>>([*:5]-[OH;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6])
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification and characterization of L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase, and L-arabinolactonase involved in an alternative pathway of L-arabinose metabolism. Novel evolutionary insight into sugar metabolism.Watanabe S, Shimada N, Tajima K, Kodaki T, Makino K2006 Nov 316950779
The oxidation of L-arabinose by Pseudomonas saccharophila.WEIMBERG R, DOUDOROFF M1955 Dec13271422