From Surf Wiki (app.surf) — the open knowledge base
3,4-dihydroxy-2-butanone-4-phosphate synthase
Class of enzymes
Class of enzymes
| Field | Value |
|---|---|
| Symbol | DHBP_synthase |
| Name | DHBP_synthase |
| image | PDB 1g58 EBI.jpg |
| caption | crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase gold derivative |
| Pfam | PF00926 |
| InterPro | IPR000422 |
| SCOP | 1iez |
The enzyme 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (RibB) catalyses the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate, the latter serving as the biosynthetic precursor for the xylene ring of riboflavin. In Photobacterium leiognathi, the riboflavin synthesis genes ribB (DHBP synthase), ribE (riboflavin synthase), ribH (lumazine synthase) and ribA (GTP cyclohydrolase II) all reside in the lux operon. RibB is sometimes found as a bifunctional enzyme with GTP cyclohydrolase II that catalyses the first committed step in the biosynthesis of riboflavin. No sequences with significant homology to DHBP synthase are found in the metazoa.
References
References
- (1997). "Vitamins and Coenzymes Part J".
- (June 2001). "Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi". Biochemical and Biophysical Research Communications.
This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.
Ask Mako anything about 3,4-dihydroxy-2-butanone-4-phosphate synthase — get instant answers, deeper analysis, and related topics.
Research with MakoFree with your Surf account
Create a free account to save articles, ask Mako questions, and organize your research.
Sign up freeThis content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.
Report