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Information on EC 2.7.11.3 - dephospho-[reductase kinase] kinase for references in articles please use BRENDA:EC2.7.11.3
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EC Tree
IUBMB Comments The enzyme is activated by AMP and is specific for its substrate. Phosphorylates and activates EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, that has been inactivated by EC 3.1.3.16, protein-serine/threonine phosphatase.
The enzyme appears in viruses and cellular organisms
Synonyms
reductase kinase kinase, amp-activated protein kinase kinase,
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AMP-activated protein kinase kinase
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hydroxymethylglutaryl coenzyme A reductase kinase kinase
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hydroxymethylglutaryl coenzyme A reductase kinase kinase (phosphorylating)
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reductase kinase kinase
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ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} = ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
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phospho group transfer
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ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase
The enzyme is activated by AMP and is specific for its substrate. Phosphorylates and activates EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, that has been inactivated by EC 3.1.3.16, protein-serine/threonine phosphatase.
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ATP + histone 2A
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poor substrate
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ATP + phosvitin
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slight activity
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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i.e. AMP-activated protein kinase
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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No substrate is hydroxymethylglutaryl-CoA reductase (NADPH)
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylates catalytic subunit of EC2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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bicyclic phosporylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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involved in regulation cascade of hydroxymethylglutaryl-CoA reductase, EC 1.1.1.34
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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important for the responses of cells to metabolic stresses such as lack of cell nutrients, hypoxia, ischemia and muscular exercise
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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bicyclic phosporylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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involved in regulation cascade of hydroxymethylglutaryl-CoA reductase, EC 1.1.1.34
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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important for the responses of cells to metabolic stresses such as lack of cell nutrients, hypoxia, ischemia and muscular exercise
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
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phosphorylation activates EC 2.7.1.109
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AMP
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allosteric activator, the allosteric effect and the promotion of phosphorylation and activation by the kinase kinase are due to binding of AMP to a single site on the kinase
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Mg2+
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requirement, actual substrate: MgATP
Mg2+
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requirement, actual substrate: MgATP
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adenosine(5')tetraphospho(5')adenosine
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i.e. AP4A, inhibits in the presence of AMP
poly(Arg)
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casein as substrate
additional information
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no inhibition by inhibitor of cAMP-dependent protein kinase
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8-Aza-9-deaza-AMP
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activation, i.e. formycin A-5'-monophosphate, can replace AMP
8-Aza-9-deaza-IMP
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slight activation, i.e. formycin B-5'-monophosphate
Mevalonolactone
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activation, in vitro and in vivo
additional information
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cAMP-independent enzyme
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additional information
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no activation by formycin A or B
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3 - 4
Sodium fluoride
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pH 7.4, 37°C
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7.4
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assay at
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30
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assay at
37
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5.6 - 5.9
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isoelectric focusing
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brenda
Sprague-Dawley
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Wistar
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Sprague-Dawley
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Wistar
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brenda
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predominant
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predominant
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predominant
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brenda
additional information
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subcellular distribution
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additional information
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subcellular distribution
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brenda
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58000
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? * 58000 + ?, catalytic alpha subunit, SDS-PAGE
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?
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? * 58000 + ?, catalytic alpha subunit, SDS-PAGE
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T172D
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site-directed mutagenesis
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-20°C, can be stored in buffer containing 50% glycerol for up to a month
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cytosolic enzyme; partial
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partial
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bacterially expressed recombinant alpha1 subunit proteins
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Ingebritsen, T.S.; Parker, R.A.; Gibson, D.M.
Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system
J. Biol. Chem.
256
1138-1144
1981
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Ingebritsen, T.S.; Lee, H.S.; Parker, R.A.; Gibson, D.M.
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
1268-1277
1978
Rattus norvegicus
brenda
Beg, Z.H.; Stonik, J.A.; Brewer, B.
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. USA
76
4375-4379
1979
Rattus norvegicus
brenda
Weekes, J.; Hawley, S.A.; Corton, J.; Shugar, D.; Hardie, D.G.
Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues
Eur. J. Biochem.
219
751-757
1994
Rattus norvegicus
brenda
Beg, Z.H.; Stonik, J.A.; Brewer, B.
In vivo modulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase, reductase kinase, and reductase kinase kinase by mevalonolactone
Proc. Natl. Acad. Sci. USA
81
7293-7297
1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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Beg, Z.H.; Stonik, J.A.; Brewer, B.
Human hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase: evidence for the regulation of enzymic activity by a bicyclic phosphorylation cascade
Biochem. Biophys. Res. Commun.
119
488-498
1984
Homo sapiens
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Hawley, S.A.; Selbert, M.A.; Goldstein, E.G.; Edelman, A.M.; Carling, D.; Hardie, D.G.
5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
J. Biol. Chem.
270
27186-27191
1995
Rattus norvegicus
brenda
Hawley, S.A.; Davison, M.; Woods, A.; Davies, S.P.; Beri, R.K.; Carling, D.; Hardie, D.G.
Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
J. Biol. Chem.
271
27879-27887
1996
Rattus norvegicus
brenda
Hamilton, S.R.; O'Donnell, J.B., Jr.; Hammet, A.; Stapleton, D.; Habinowski, S.A.; Means, A.R.; Kemp, B.E.; Witters, L.A.
AMP-activated protein kinase kinase: detection with recombinant AMPK alpha1 subunit
Biochem. Biophys. Res. Commun.
293
892-898
2002
Rattus norvegicus
brenda
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2.7.11.3 dephospho-[reductase kinase] kinase
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