Dephospho-(reductase kinase) kinase: Difference between revisions
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]]. |
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]]. |
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This enzyme belongs to the family of [[transferase]]s, specifically those transferring a phosphate group to the sidechain [[oxygen]] atom of [[serine]] or [[threonine]] residues in [[protein]]s ([[protein-serine/threonine kinase]]s). The systematic name of this enzyme class is '''ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase'''. Other names in common use include '''AMP-activated kinase''', '''AMP-activated protein kinase kinase''', '''hydroxymethylglutaryl coenzyme A reductase kinase kinase''', '''hydroxymethylglutaryl coenzyme A reductase kinase kinase''', '''(phosphorylating)''', '''reductase kinase''', '''reductase kinase kinase''', and '''STK30'''. |
This enzyme belongs to the family of [[transferase]]s, specifically those transferring a phosphate group to the sidechain [[oxygen]] atom of [[serine]] or [[threonine]] residues in [[protein]]s ([[protein-serine/threonine kinase]]s). The systematic name of this enzyme class is '''ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase'''. Other names in common use include '''AMP-activated kinase''', '''AMP-activated protein kinase kinase''', '''hydroxymethylglutaryl coenzyme A reductase kinase kinase''', '''hydroxymethylglutaryl coenzyme A reductase kinase kinase''', '''(phosphorylating)''', '''reductase kinase''', '''reductase kinase kinase''', and '''STK30'''. |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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* {{cite journal | author = Beg ZH, Stonik JA, Brewer HB Jr | |
* {{cite journal | author = Beg ZH, Stonik JA, Brewer HB Jr | year = 1979 | title = Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase | journal = Proc. Natl. Acad. Sci. U. S. A. | volume = 76 | pages = 4375–9 | pmid = 291971 | doi = 10.1073/pnas.76.9.4375 | issue = 9 | pmc = 411577 }} |
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* {{cite journal | author = Ingebritsen TS, Lee HS, Parker RA, Gibson DM | |
* {{cite journal | author = Ingebritsen TS, Lee HS, Parker RA, Gibson DM | year = 1978 | title = Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation | journal = Biochem. Biophys. Res. Commun. | volume = 81 | pages = 1268–77 | pmid = 666819 | doi = 10.1016/0006-291X(78)91273-1 | issue = 4 }} |
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* {{cite journal | author = Beg ZH, Stonik JA, Brewer HB Jr | |
* {{cite journal | author = Beg ZH, Stonik JA, Brewer HB Jr | year = 1985 | title = Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and modulation of its enzymic activity by calcium-activated and phospholipid-dependent protein kinase | journal = J. Biol. Chem. | volume = 260 | pages = 1682–7 | pmid = 3155737 | issue = 3 }} |
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* {{cite journal | author = Clarke PR, Hardie DG | |
* {{cite journal | author = Clarke PR, Hardie DG | year = 1990 | title = Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver | journal = EMBO J. | volume = 9 | pages = 2439–46 | pmid = 2369897 | issue = 8 | pmc = 552270 }} |
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* {{cite journal | author = Sato R, Goldstein JL, Brown MS | |
* {{cite journal | author = Sato R, Goldstein JL, Brown MS | year = 1993 | title = Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA reductase prevents phosphorylation by AMP-activated kinase and blocks inhibition of sterol synthesis induced by ATP depletion | journal = Proc. Natl. Acad. Sci. U. S. A. | volume = 90 | pages = 9261–5 | pmid = 8415689 | doi = 10.1073/pnas.90.20.9261 | issue = 20 | pmc = 47547 }} |
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[[Category:EC 2.7.11]] |
[[Category:EC 2.7.11]] |
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[[Category:Enzymes of unknown structure]] |
[[Category:Enzymes of unknown structure]] |
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Revision as of 06:45, 11 July 2011
dephospho-[reductase kinase] kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.11.3 | ||||||||
CAS no. | 72060-33-4 | ||||||||
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 | ||||||||
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In enzymology, a dephospho-[reductase kinase] kinase (EC 2.7.11.3) is an enzyme that catalyzes the chemical reaction
- ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
Thus, the two substrates of this enzyme are ATP and [[dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]], whereas its two products are ADP and [[{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]].
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase. Other names in common use include AMP-activated kinase, AMP-activated protein kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, (phosphorylating), reductase kinase, reductase kinase kinase, and STK30.
References
- Beg ZH, Stonik JA, Brewer HB Jr (1979). "Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase". Proc. Natl. Acad. Sci. U. S. A. 76 (9): 4375–9. doi:10.1073/pnas.76.9.4375. PMC 411577. PMID 291971.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - Ingebritsen TS, Lee HS, Parker RA, Gibson DM (1978). "Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation". Biochem. Biophys. Res. Commun. 81 (4): 1268–77. doi:10.1016/0006-291X(78)91273-1. PMID 666819.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - Beg ZH, Stonik JA, Brewer HB Jr (1985). "Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and modulation of its enzymic activity by calcium-activated and phospholipid-dependent protein kinase". J. Biol. Chem. 260 (3): 1682–7. PMID 3155737.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - Clarke PR, Hardie DG (1990). "Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver". EMBO J. 9 (8): 2439–46. PMC 552270. PMID 2369897.
- Sato R, Goldstein JL, Brown MS (1993). "Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA reductase prevents phosphorylation by AMP-activated kinase and blocks inhibition of sterol synthesis induced by ATP depletion". Proc. Natl. Acad. Sci. U. S. A. 90 (20): 9261–5. doi:10.1073/pnas.90.20.9261. PMC 47547. PMID 8415689.
{{cite journal}}
: CS1 maint: multiple names: authors list (link)