Gluconolactonase
| gluconolactonase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
![]() Gluconolactonase homodimer, Xanthomonas campestris[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.1.17 | ||||||||
| CAS no. | 9012-73-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Gluconolactonase (EC 3.1.1.17) is an enzyme that catalyzes the reaction
The enzyme characterised from baker's yeast hydrolyses glucono-δ-lactone to give gluconic acid.[2][3][4] Its structure has been determined by X-ray crystallography.[1]
This enzyme is a hydrolase, specifically one acting on carboxylic ester bonds. The systematic name is D-glucono-1,5-lactone lactonohydrolase. Other names in common use include lactonase, aldonolactonase, glucono-δ-lactonase, and gulonolactonase.[5]
References
- 1 2 Chen, Cheng-Nan; Chin, Ko-Hsin; Wang, Andrew H.-J.; Chou, Shan-Ho (2008). "The First Crystal Structure of Gluconolactonase Important in the Glucose Secondary Metabolic Pathways". Journal of Molecular Biology. 384 (3): 604–614. doi:10.1016/j.jmb.2008.09.055. PMID 18848569.
- ↑ Brodie AF, Lipmann F (1955). "Identification of a gluconolactonase". J. Biol. Chem. 212 (2): 677–85. doi:10.1016/S0021-9258(18)71006-5. PMID 14353869.
- ↑ Bublitz C; Lehninger AL (1961). "The role of aldonolactonase in the conversion of L-gulonate to L-ascorbate". Biochim. Biophys. Acta. 47 (2): 288–297. doi:10.1016/0006-3002(61)90289-X.
- ↑ Suzuki K, Kawada M, Shimazono N. "Soluble lactonase. Identity of lactonase I and aldonolactonase with gluconolactonase". J. Biochem. 49: 448–449. doi:10.1093/oxfordjournals.jbchem.a127326.
- ↑ Enzyme 3.1.1.17 at KEGG Pathway Database.
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