Glycerol kinase: Difference between revisions
Jump to navigation
Jump to search
m (I fixed a typo. "Glycerol 3-Phosphate Dehydrogenae" to "Glycerol 3-Phosphate Dehydrogenase") |
imported>Natureium (ce) |
||
| Line 29: | Line 29: | ||
|LocusSupplementaryData= | |LocusSupplementaryData= | ||
}} | }} | ||
'''Glycerol kinase''' is a [[phosphotransferase]] [[enzyme]] involved in [[triglyceride]]s and [[glycerophospholipid]]s synthesis. | '''Glycerol kinase''', encoded by the gene ''GK'', is a [[phosphotransferase]] [[enzyme]] involved in [[triglyceride]]s and [[glycerophospholipid]]s synthesis. | ||
Glycerol kinase catalyzes the transfer of a phosphate from [[adenosine triphosphate|ATP]] to [[glycerol]] thus forming [[glycerol 3-phosphate]]: | Glycerol kinase catalyzes the transfer of a phosphate from [[adenosine triphosphate|ATP]] to [[glycerol]] thus forming [[glycerol 3-phosphate]]: | ||
| Line 41: | Line 41: | ||
==Enzyme regulation== | ==Enzyme regulation== | ||
This protein may use the [[morpheein]] model of [[allosteric regulation]].<ref name=pmid22182754>{{cite journal | | This protein may use the [[morpheein]] model of [[allosteric regulation]].<ref name=pmid22182754>{{cite journal | vauthors = Selwood T, Jaffe EK | title = Dynamic dissociating homo-oligomers and the control of protein function | journal = Archives of Biochemistry and Biophysics | volume = 519 | issue = 2 | pages = 131–43 | date = March 2012 | pmid = 22182754 | pmc = 3298769 | doi = 10.1016/j.abb.2011.11.020 }}</ref> | ||
==Structure== | ==Structure== | ||
| Line 47: | Line 47: | ||
Glycerol Kinase (alternative name, ATP:glycerol 3-phosphotransferase or Glycerokinase) adopts a [[rnase H|ribonuclease H]]-like fold consisting of an alpha-beta 2-layer sandwich of [[CATH]] family 3.30.420.40. {{As of|2010|03}}, there were 20 structures of this protein in the PDB, most of which are homodimeric. | Glycerol Kinase (alternative name, ATP:glycerol 3-phosphotransferase or Glycerokinase) adopts a [[rnase H|ribonuclease H]]-like fold consisting of an alpha-beta 2-layer sandwich of [[CATH]] family 3.30.420.40. {{As of|2010|03}}, there were 20 structures of this protein in the PDB, most of which are homodimeric. | ||
==See also== | == See also == | ||
* [[Glycerol]] | * [[Glycerol]] | ||
* [[Kinase]] | * [[Kinase]] | ||
==External links== | == External links == | ||
* {{MeshName|Glycerol+Kinase}} | * {{MeshName|Glycerol+Kinase}} | ||
==References== | == References == | ||
{{reflist}} | {{reflist}} | ||
{{Kinases}} | {{Kinases}} | ||
| Line 64: | Line 62: | ||
[[Category:EC 2.7.1]] | [[Category:EC 2.7.1]] | ||
{{2.7-enzyme-stub}} | {{2.7-enzyme-stub}} | ||
Revision as of 16:07, 12 March 2018
| glycerol kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:1glf.jpg glycerol kinase dimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC number | 2.7.1.30 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| glycerol kinase | |
|---|---|
| Identifiers | |
| Symbol | GK |
| Entrez | 2710 |
| HUGO | 4289 |
| OMIM | 300474 |
| RefSeq | NM_000167 |
| UniProt | P32189 |
| Other data | |
| EC number | 2.7.1.30 |
| Locus | Chr. X p21.3 |
Glycerol kinase, encoded by the gene GK, is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis.
Glycerol kinase catalyzes the transfer of a phosphate from ATP to glycerol thus forming glycerol 3-phosphate:
- ATP + glycerol <=> ADP + sn-glycerol 3-phosphate
Adipocytes lack glycerol kinase so they cannot metabolize the glycerol produced during triacyl glycerol degradation. This glycerol is instead shuttled to the liver via the blood where it is:
- phosphorylated by glycerol kinase to glycerol 3-phosphate
- Converted from Glycerol 3-Phosphate to dihydroxyacetone phosphate (DHAP) via Glycerol 3-Phosphate Dehydrogenase. DHAP can participate in glycolysis or gluconeogenesis.
Enzyme regulation
This protein may use the morpheein model of allosteric regulation.[1]
Structure
Glycerol Kinase (alternative name, ATP:glycerol 3-phosphotransferase or Glycerokinase) adopts a ribonuclease H-like fold consisting of an alpha-beta 2-layer sandwich of CATH family 3.30.420.40. As of March 2010[update], there were 20 structures of this protein in the PDB, most of which are homodimeric.
See also
External links
- Glycerol+Kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
References
- ↑ Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
| This EC 2.7 enzyme-related article is a stub. You can help Wikipedia by expanding it. |
Categories:
- Pages with broken file links
- Protein pages needing a picture
- Genes on human chromosome X
- Articles containing potentially dated statements from March 2010
- Articles with invalid date parameter in template
- All articles containing potentially dated statements
- Portal templates with all redlinked portals
- EC 2.7.1
- All stub articles
- EC 2.7 stubs