Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline fumonisin B1 Identifier CHEBI:62554 Charge -3 Formula C34H56NO15 InChIKeyhelp_outline UVBUBMSSQKOIBE-DSLOAKGESA-K SMILEShelp_outline CCCC[C@@H](C)[C@@H](OC(=O)C[C@@H](CC([O-])=O)C([O-])=O)[C@H](C[C@@H](C)C[C@H](O)CCCC[C@@H](O)C[C@H](O)[C@H](C)[NH3+])OC(=O)C[C@@H](CC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline tricarballylate Identifier CHEBI:62517 Charge -3 Formula C6H5O6 InChIKeyhelp_outline KQTIIICEAUMSDG-UHFFFAOYSA-K SMILEShelp_outline [O-]C(=O)CC(CC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2S,3S,5R,10R,12S,14S,15R,16R)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol Identifier CHEBI:62526 Charge 1 Formula C22H48NO5 InChIKeyhelp_outline UWWVLQOLROBFTD-GADKELDLSA-O SMILEShelp_outline CCCC[C@@H](C)[C@@H](O)[C@@H](O)C[C@@H](C)C[C@H](O)CCCC[C@@H](O)C[C@H](O)[C@H](C)[NH3+] 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 H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:30363 | RHEA:30364 | RHEA:30365 | RHEA:30366 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Degradation of fumonisin B1 by the consecutive action of two bacterial enzymes.
Heinl S., Hartinger D., Thamhesl M., Vekiru E., Krska R., Schatzmayr G., Moll W.-D., Grabherr R.
Detoxification of the mycotoxin fumonisin B(1) comprises at least two enzymatic steps, an initial deesterification reaction, followed by deamination of the resulting hydrolyzed fumonisin B(1). In this study, two genes that are responsible for degradation of fumonisin B(1) by the bacterium Sphingop ... >> More
Detoxification of the mycotoxin fumonisin B(1) comprises at least two enzymatic steps, an initial deesterification reaction, followed by deamination of the resulting hydrolyzed fumonisin B(1). In this study, two genes that are responsible for degradation of fumonisin B(1) by the bacterium Sphingopyxis sp. MTA144 were identified within a gene cluster, assumed to be associated with fumonisin degradation. The first gene encodes a protein which shows similarity to carboxylesterases, type B. The second gene encodes a polypeptide homologous to aminotransferases, class III. The two genes were isolated and expressed heterologously. The effect of the recombinant enzymes on fumonisin B(1) and hydrolyzed fumonisin B(1) was determined. The recombinant carboxylesterase was shown to catalyze the deesterification of fumonisin B(1) to hydrolyzed fumonisin B(1). The heterologously expressed aminotransferase was shown to deaminate hydrolyzed fumonisin B(1) in the presence of pyruvate and pyridoxal phosphate. We propose that the consecutive action of these two enzymes is sufficient for fumonisin B(1) detoxification. The results of this work provide a basis for the development of an enzymatic detoxification process for fumonisin B(1) in food and animal feed, especially under oxygen limited conditions, as they are found, e.g. in ensilaged forage or in the intestinal tract of animals. << Less
J. Biotechnol. 145:120-129(2010) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.