Pantoate 4-dehydrogenase
The following article will explore the impact of Pantoate 4-dehydrogenase on contemporary society. Pantoate 4-dehydrogenase has been a topic of interest and debate over the years, generating conflicting opinions among experts and the general public. This figure/person/theme has left an indelible mark on popular culture, politics, economics, and many other aspects of modern society. Through a detailed analysis we will try to shed light on the influence of Pantoate 4-dehydrogenase in different areas, as well as examine its relevance in the current context. Various perspectives will be addressed and arguments will be presented that invite reflection and debate on this topic.
| pantoate 4-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.106 | ||||||||
| CAS no. | 37250-38-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a pantoate 4-dehydrogenase (EC 1.1.1.106) is an enzyme that catalyzes the chemical reaction
- (R)-pantoate + NAD+ (R)-4-dehydropantoate + NADH + H+
Thus, the two substrates of this enzyme are (R)-pantoate and NAD+, whereas its 3 products are (R)-4-dehydropantoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-pantoate:NAD+ 4-oxidoreductase. Other names in common use include pantoate dehydrogenase, pantothenase, and D-pantoate:NAD+ 4-oxidoreductase. This enzyme participates in pantothenate and coa biosynthesis.
References
- Goodhue CT, Snell EE (1966). "The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid". Biochemistry. 5 (2): 403–8. doi:10.1021/bi00866a003. PMID 4287370.
