Gluconolactonase

gluconolactonase
Gluconolactonase homodimer, Xanthomonas campestris[1]
Identifiers
EC no.3.1.1.17
CAS no.9012-73-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Gluconolactonase (EC 3.1.1.17) is an enzyme that catalyzes the reaction

 
H2O
 
Rightward reaction arrow with minor substrate(s) from top left
 
 
 

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. 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ Enzyme 3.1.1.17 at KEGG Pathway Database.