Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline β-lactose Identifier CHEBI:36218 (Beilstein: 90841; CAS: 5965-66-2) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline GUBGYTABKSRVRQ-DCSYEGIMSA-N SMILEShelp_outline OC[C@H]1O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O2 Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 426 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline lactobiono-1,5-lactone Identifier CHEBI:143068 Charge 0 Formula C12H20O11 InChIKeyhelp_outline FSICMNGKCHFHGP-AMTLMPIISA-N SMILEShelp_outline C1([C@@H]([C@H]([C@@H]([C@H](O1)CO)O[C@H]2[C@@H]([C@H]([C@H]([C@H](O2)CO)O)O)O)O)O)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59352 | RHEA:59353 | RHEA:59354 | RHEA:59355 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline |
Publications
-
A novel carbohydrate:acceptor oxidoreductase from Microdochium nivale.
Xu F., Golightly E.J., Fuglsang C.C., Schneider P., Duke K.R., Lam L., Christensen S., Brown K.M., Joergensen C.T., Brown S.H.
A Microdochium nivale carbohydrate:acceptor oxidoreductase was purified, cloned, heterologously expressed, and characterized. The gene encoding the protein showed one intron, and the ORF showed a sequence with low homology (< or = 25% identity or 65% similarity) to other known flavin-containing ca ... >> More
A Microdochium nivale carbohydrate:acceptor oxidoreductase was purified, cloned, heterologously expressed, and characterized. The gene encoding the protein showed one intron, and the ORF showed a sequence with low homology (< or = 25% identity or 65% similarity) to other known flavin-containing carbohydrate oxidases. The maturation of the protein required the cleavage of a tetrameric propeptide in addition to an 18 amino-acid signal peptide. The enzyme was found to have a relative molecular mass of 55 000 Da, an isoelectric point of 9, and one FAD per protein. It could oxidize mono-, oligo-, or polymeric saccharides, and transfer their electrons to O2 or other acceptors. When D-glucose served as electron-donating substrate, an activity of 2 s(-1) was observed at pH 5.5 and 23 degrees C. Among various oligosaccharides, the enzyme preferred tetrameric dextrins, indicating a favorable interaction of four linked glucose units with the substrate pocket. The unique structure and ability of oxidizing oligo/polymeric saccharides suggest a promising prospect of this enzyme for various industrial/medicinal applications. << Less
Eur. J. Biochem. 268:1136-1142(2001) [PubMed] [EuropePMC]
This publication is cited by 11 other entries.
Comments
Published in: Kulys, J., Tetianec, L. and Schneider, P. Specificity and kinetic parameters of recombinant