SGD Paper 
Zhang M and Robertus JD (2002) Molecular cloning and characterization of a full-length flavin-dependent monooxygenase from yeast. Arch Biochem Biophys 403(2):277-83
Abstract: Eucaryotes contain a class of enzymes called flavin-dependent monooxygenases (FMOs). Unlike mammals, yeast have only a single isoform-yFMO. Deletion mutants suggested that yFMO may play a role in folding proteins which contain disulfide bonds. Recently we detected two nucleotide errors in the GenBank sequences attributed to the yFMO gene. This previously led us to express and characterize a 373-residue catalytically active protein instead of the correct 432-residue enzyme. Here we report the sequencing, expression, and enzyme characterization of the full-length form of yFMO. Comparison of the two forms of yFMO showed similar pH profiles and K(m), K(cat), and V(max) values using glutathione as a substrate. These results indicate that the full-length yeast FMO has biochemical and catalytic properties similar to those of the truncated protein. Therefore, it is likely that the hypotheses concerning the enzyme's function proposed earlier are still valid.
| Status: Published | Type: Journal Article | PubMed ID: 12139977 |
Topics addressed in this paper
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
| Topics | Genes linked to topics |
|---|---|
| FMO1 | |
| DNA/RNA Sequence Features |  |
| Function/Process | |
| Primary Literature | |
| Protein Physical Properties | |
| Substrates/Ligands/Cofactors | |
