| EC |
1.5.3.26 |
| Accepted name: |
fructosyl amine oxidase (fructosamine-forming) |
| Reaction: |
an N-(1-deoxy-D-fructos-1-yl)amine + O2 + H2O = (1-deoxy-D-fructos-1-yl)amine + an aldehyde + H2O2 |
| Systematic name: |
N-(1-deoxy-D-fructos-1-yl)amine:oxygen oxidoreductase (fructosamine-forming) |
| Comments: |
Reducing sugars such as glucose react with amino groups in proteins via the spontaeous Maillard reaction, forming an unstable product that undergoes spontaneous rearrangement to a keto amine compound. These reactions are known as glycation reactions, and the stable products are known as Amadori products. This enzyme, characterized from a Pseudomonas sp. strain, cleaves the Amadori products at the alkylamine bond. All other known fructosyl amine oxidases cleave the ketoamine bond (cf. EC 1.5.3.25, fructosyl amine oxidase (glucosone-forming)). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Gerhardinger, C., Marion, M.S., Rovner, A., Glomb, M. and Monnier, V.M. Novel degradation pathway of glycated amino acids into free fructosamine by a Pseudomonas sp. soil strain extract. J. Biol. Chem. 270 (1995) 218–224. [DOI] [PMID: 7814378] |
| 2. |
Saxena, A.K., Saxena, P. and Monnier, V.M. Purification and characterization of a membrane-bound deglycating enzyme (1-deoxyfructosyl alkyl amino acid oxidase, EC 1.5.3) from a Pseudomonas sp. soil strain. J. Biol. Chem. 271 (1996) 32803–32809. [DOI] [PMID: 8955117] |
| 3. |
Wu, X. and Monnier, V.M. Enzymatic deglycation of proteins. Arch. Biochem. Biophys. 419 (2003) 16–24. [DOI] [PMID: 14568004] |
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| [EC 1.5.3.26 created 2022] |
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