Biosynthesis of Riboflavin - Journal of Biological Chemistry
This entry describes the riboflavin biosynthesis protein (ribD) as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region that is shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins that may be related to the riboflavin biosynthesis protein contain only the C-terminal domain.
to inhibitors of riboflavin biosynthesis.
Saccharomyces cerevisiae riboflavin, FMN and FAD biosynthesis
Accordingly, six genes (rib genes), which encode from enzymes of riboflavin biosynthesis starting from GTP, were found in the yeast Saccharomyces cerevisiae and isolated.
PubMed - National Center for Biotechnology Information
Specifically, the invention relates to the genes for riboflavin biosynthesis in yeast, the proteins encoded therewith and genetic engineering process for the preparation of riboflavin using these genes and gene products.