Difference between revisions of "Sorbitol dehydrogenase"
(Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|Sord, SDH, L-iditol 2-dehydrogenase|[https://www.uniprot.org/uniprot/P27867 P27867]|Rattus norvegicus|Cys45, Cy...") |
(→Protein Function) |
||
| Line 9: | Line 9: | ||
Sorbitol dehydrogenase is an enzyme include in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. <br/> | Sorbitol dehydrogenase is an enzyme include in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. <br/> | ||
Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is:<br/> | Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is:<br/> | ||
| − | + | <div align="center">Sorbitol + NAD+ --> fructose + NADH + H+.</div> | |
A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietary sorbitol, though sorbitol is known not to be absorbed as well in the intestine as its related compounds glucose and fructose, and is usually found in quite small amounts in the diet (except when used as an artificial sweetener). (From Wikipedia) <br/> | A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietary sorbitol, though sorbitol is known not to be absorbed as well in the intestine as its related compounds glucose and fructose, and is usually found in quite small amounts in the diet (except when used as an artificial sweetener). (From Wikipedia) <br/> | ||
Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. (From Uniprot) <br/> | Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. (From Uniprot) <br/> | ||
Revision as of 02:01, 18 August 2019
| Basic Information | |
|---|---|
| Short Name | Sord, SDH, L-iditol 2-dehydrogenase |
| UNP ID | P27867 |
| Organism | Rattus norvegicus |
| Cys Site | Cys45, Cys130 |
| Family/Domain |
Zinc-binding dehydrogenase, Zinc-containing alcohol dehydrogenase family |
| Known Ligand | Ligand list |
| Function Type | Transcription Related |
Summary
Protein Function
Sorbitol dehydrogenase is an enzyme include in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP.
Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is:
A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietary sorbitol, though sorbitol is known not to be absorbed as well in the intestine as its related compounds glucose and fructose, and is usually found in quite small amounts in the diet (except when used as an artificial sweetener). (From Wikipedia)
Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. (From Uniprot)
Cys Function & Property
Cys45 is the metal binding site of Sord. And two regions, residues 90–110 and 120–140, are very important for the stability and binding between subunits in mammalian SDHs. (PMID: 22752181, 17952367)
- Hydrophobic property:
- SASA：
- Cys45: Unknown
- Cys120: Unknown
Protein Sequence
MAAPAKGENL SLVVHGPGDI RLENYPIPEL GPNDVLLKMH SVGICGSDVH
YWEHGRIGDF VVKKPMVLGH EAAGTVTKVG PMVKHLKPGD RVAIEPGVPR
EIDEFCKIGR YNLTPSIFFC ATPPDDGNLC RFYKHSADFC YKLPDSVTFE
EGALIEPLSV GIYACRRGSV SLGNKVLVCG AGPIGIVTLL VAKAMGASQV
VVIDLSASRL AKAKEVGADF TIQVAKETPH DIAKKVESVL GSKPEVTIEC
TGAESSVQTG IYATHSGGTL VVVGMGPEMI NLPLVHAAVR EVDIKGVFRY
CNTWPMAVSM LASKTLNVKP LVTHRFPLEK AVEAFETAKK GLGLKVMIKC
DPNDQNP
Structural Information
- Known structure with covalent ligand:
- Unknown
- Protein structure:
- Unknown
Related Pathway
Experimental Evidence
- MALDI-TOF/MS, Cys Modification Assay
Reference
- Kanda H, Toyama T, Shinohara-Kanda A, et al. S-Mercuration of rat sorbitol dehydrogenase by methylmercury causes its aggregation and the release of the zinc ion from the active site[J]. Archives of toxicology, 2012, 86(11): 1693-1702. 22752181
