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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 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.11 Protein-serine/threonine kinases
2.7.11.3 dephospho-[reductase kinase] kinase
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
- 2.7.11.3
-
ampkks
- hmg-coa
-
endurance-trained
-
strad
- phosphoprotein
-
endurance
- alpha1
-
quadriceps
-
soleus
-
3-hydroxy-3-methylglutaryl
-
1.1.1.34
- cholesterol
- citrate
- mevalonolactone
-
sedentary
- mevalonate
-
atp-mg
- glycol
-
bicyclic
- phosphatases
Reaction Schemes
showSynonyms
reductase kinase kinase, amp-activated protein kinase kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AMP-activated protein kinase kinase
-
-
-
-
EC 2.7.1.110
-
-
formerly
-
hydroxymethylglutaryl coenzyme A reductase kinase kinase
-
-
-
-
hydroxymethylglutaryl coenzyme A reductase kinase kinase (phosphorylating)
-
-
-
-
reductase kinase kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} = ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
72060-33-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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]
-
Substrates: -
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: -
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: i.e. AMP-activated protein kinase
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: No substrate is hydroxymethylglutaryl-CoA reductase (NADPH)
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylates catalytic subunit of EC2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: bicyclic phosphorylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: involved in regulation cascade of hydroxymethylglutaryl-CoA reductase, EC 1.1.1.34
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: important for the responses of cells to metabolic stresses such as lack of cell nutrients, hypoxia, ischemia and muscular exercise
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: -
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: -
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: bicyclic phosphorylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: involved in regulation cascade of hydroxymethylglutaryl-CoA reductase, EC 1.1.1.34
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: important for the responses of cells to metabolic stresses such as lack of cell nutrients, hypoxia, ischemia and muscular exercise
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]
-
Substrates: phosphorylation activates EC 2.7.1.109
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine(5')tetraphospho(5')adenosine
-
i.e. AP4A, inhibits in the presence of AMP
additional information
-
no inhibition by inhibitor of cAMP-dependent protein kinase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-Aza-9-deaza-AMP
-
activation, i.e. formycin A-5'-monophosphate, can replace AMP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
brenda
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
EXTERNAL LINKS (specific for EC-Number 2.7.11.3)
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