Pyridoxine 4-dehydrogenase: Difference between revisions
Content deleted Content added
m replaced {{oxidoreductases}} with {{Alcohol oxidoreductases}} |
No edit summary |
||
| (5 intermediate revisions by 3 users not shown) | |||
| Line 1: | Line 1: | ||
{{enzyme |
{{infobox enzyme |
||
| Name = pyridoxine 4-dehydrogenase |
| Name = pyridoxine 4-dehydrogenase |
||
| EC_number = 1.1.1.65 |
| EC_number = 1.1.1.65 |
||
| CAS_number = 9028-64-2 |
| CAS_number = 9028-64-2 |
||
| GO_code = 0050236 |
|||
| IUBMB_EC_number = 1/1/1/65 |
|||
| |
| image = |
||
| |
| width = |
||
| |
| caption = |
||
| caption = |
|||
}} |
}} |
||
In [[enzymology]], a '''pyridoxine 4-dehydrogenase''' ({{EC number|1.1.1.65}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
In [[enzymology]], a '''pyridoxine 4-dehydrogenase''' ({{EC number|1.1.1.65}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
||
| Line 15: | Line 14: | ||
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[pyridoxine]] and [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[pyridoxal]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]]. |
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[pyridoxine]] and [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[pyridoxal]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]]. |
||
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of |
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donors with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptors. The [[List of enzymes|systematic name]] of this enzyme class is '''pyridoxine:NADP<sup>+</sup> 4-oxidoreductase'''. Other names in common use include '''pyridoxin dehydrogenase''', '''pyridoxol dehydrogenase''', and '''pyridoxine dehydrogenase'''. This enzyme participates in [[vitamin B6|vitamin B<sub>6</sub> metabolism]]. |
||
==References== |
==References== |
||
{{reflist|1}} |
{{reflist|1}} |
||
* {{cite journal | |
* {{cite journal | vauthors = Holzer H, Schneider S | date = 1961 | title = [Purification and characterization of a TPN-dependent pyridoxol dehydrogenase from brewers yeast.] | language=German | journal = Biochim. Biophys. Acta | volume = 48 | pages = 71–6 | pmid = 13715611 | doi = 10.1016/0006-3002(61)90516-9 }} |
||
{{Alcohol oxidoreductases}} |
{{Alcohol oxidoreductases}} |
||
{{ |
{{Enzymes}} |
||
{{Portal bar|Biology|border=no}} |
|||
[[Category:EC 1.1.1]] |
[[Category:EC 1.1.1]] |
||
Latest revision as of 13:28, 1 June 2024
| pyridoxine 4-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.65 | ||||||||
| CAS no. | 9028-64-2 | ||||||||
| 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 pyridoxine 4-dehydrogenase (EC 1.1.1.65) is an enzyme that catalyzes the chemical reaction
- pyridoxine + NADP+ pyridoxal + NADPH + H+
Thus, the two substrates of this enzyme are pyridoxine and NADP+, whereas its 3 products are pyridoxal, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD+ or NADP+ as acceptors. The systematic name of this enzyme class is pyridoxine:NADP+ 4-oxidoreductase. Other names in common use include pyridoxin dehydrogenase, pyridoxol dehydrogenase, and pyridoxine dehydrogenase. This enzyme participates in vitamin B6 metabolism.
References
[edit]- Holzer H, Schneider S (1961). "[Purification and characterization of a TPN-dependent pyridoxol dehydrogenase from brewers yeast.]". Biochim. Biophys. Acta (in German). 48: 71–6. doi:10.1016/0006-3002(61)90516-9. PMID 13715611.
