Dephospho-(reductase kinase) kinase: Difference between revisions

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dephospho-[reductase kinase] kinase
dephospho-[reductase kinase] kinase
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EC no.	2.7.11.3
CAS no.	72060-33-4
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MetaCyc	metabolic pathway
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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}

\rightleftharpoons

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. Bibcode:1979PNAS...76.4375B. doi:10.1073/pnas.76.9.4375. PMC 411577. PMID 291971.
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.
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. doi:10.1016/S0021-9258(18)89648-X. PMID 3155737.
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. doi:10.1002/j.1460-2075.1990.tb07420.x. 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. Bibcode:1993PNAS...90.9261S. doi:10.1073/pnas.90.20.9261. PMC 47547. PMID 8415689.

This EC 2.7 enzyme-related article is a stub. You can help Wikipedia by expanding it.

@@ Line 1: / Line 1: @@
-{{enzyme
+{{infobox enzyme
-| Name = dephospho-[reductase kinase] kinase
+| Name       = dephospho-[reductase kinase] kinase
-| EC_number = 2.7.11.3
+| EC_number  = 2.7.11.3
 | CAS_number = 72060-33-4
+| GO_code    = 0047848
-| IUBMB_EC_number = 2/7/11/3
-| GO_code = 0047848
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
 In [[enzymology]], a '''dephospho-[reductase kinase] kinase''' ({{EC number|2.7.11.3}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
-:ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} <math>\rightleftharpoons</math> ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
+:ATP + dephospho-<nowiki/>{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} <math>\rightleftharpoons</math> ADP + {[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}]].
+Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[dephospho-<nowiki/>{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]].
-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 [[List of enzymes|systematic name]] of this enzyme class is '''ATP:dephospho-<nowiki/>{[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==
-{{reflist|1}}
+{{Reflist}}
-* {{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&ndash;9  | pmid = 291971 | doi = 10.1073/pnas.76.9.4375 | issue = 9 | pmc = 411577 }}
+* {{cite journal | vauthors = 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&ndash;9  | pmid = 291971 | doi = 10.1073/pnas.76.9.4375 | issue = 9 | pmc = 411577 | bibcode = 1979PNAS...76.4375B | doi-access = free }}
-* {{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&ndash;77  | pmid = 666819 | doi = 10.1016/0006-291X(78)91273-1 | issue = 4 }}
+* {{cite journal | vauthors = 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&ndash;77  | pmid = 666819 | doi = 10.1016/0006-291X(78)91273-1 | issue = 4 }}
-* {{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&ndash;7  | pmid = 3155737 | issue = 3 }}
+* {{cite journal | vauthors = 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&ndash;7  | pmid = 3155737 | issue = 3 | doi = 10.1016/S0021-9258(18)89648-X | doi-access = free }}
-* {{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&ndash;46  | pmid = 2369897 | issue = 8 | pmc = 552270 }}
+* {{cite journal | vauthors = 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&ndash;46  | pmid = 2369897 | issue = 8 | doi = 10.1002/j.1460-2075.1990.tb07420.x | pmc = 552270 }}
-* {{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&ndash;5  | pmid = 8415689 | doi = 10.1073/pnas.90.20.9261 | issue = 20 | pmc = 47547 }}
+* {{cite journal | vauthors = 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&ndash;5  | pmid = 8415689 | doi = 10.1073/pnas.90.20.9261 | issue = 20 | pmc = 47547 | bibcode = 1993PNAS...90.9261S | doi-access = free }}
 {{Serine/threonine-specific protein kinases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
-{{enzyme-stub}}
 [[Category:EC 2.7.11]]
 [[Category:Enzymes of unknown structure]]
+{{2.7-enzyme-stub}}

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)