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Information on EC 2.7.11.31 - [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase

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EC Tree
IUBMB Comments
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) . Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase . GTP can act instead of ATP
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This record set is specific for:
UNIPROT: P80386
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
adenosine monophosphate-activated protein kinase, amp-activated kinase, 5'-amp-activated protein kinase, prkaa1, snf1 kinase, adenosine 5'-monophosphate-activated protein kinase, ampkalpha1, reductase kinase, aak-2, ampk alpha2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AMP-activated protein kinase
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3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
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3-hydroxy-3-methylglutaryl-CoA reductase kinase
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AMP-activated protein kinase
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AMPK
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beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
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hydroxymethylglutaryl coenzyme A reductase kinase
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hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating)
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reductase kinase
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[hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphotransferase
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) [5]. Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase [7]. GTP can act instead of ATP [4]
CAS REGISTRY NUMBER
COMMENTARY hide
172522-01-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
show the reaction diagram
i.e. SAMS peptide
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the AMPK beta-subunit CBM has a beta-sandwich fold with the conserved residues Trp100, Lys126 and Trp133 (residue numbers according to beta1-CBM), classifying it under the CBM48 family
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AAKB1_RAT
270
0
30394
Swiss-Prot
other Location (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
AMPK is heterotrimer with alphabetagamma structure
trimer
heterotrimer, complex structure determination and analysis by mass spectrometry, dynamic light and small-angle X-ray scattering and transmission electrom microscopy, modeling, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified subunit beta1 carbohydrate-binding module CBD in complex with glucosyl-beta-cyclodextrin, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 13 mg/ml protein in 20 mM HEPES, pH 7.0, and 6 mM gBCD, with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate, 25% w/v PEG 8000, and 0.1 M sodium acetate, pH 4.5, X-ray diffraction structure determination and analysis at 1.72 A resolution, molecular replacement
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged subunit beta1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, anion exchange chromatography, and ultrafiltration
recombinant untagged protein by automated multidimensional purification including adsorption chromatography and gel filtration, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of beta1 subunit alone or in combination with other subunits in Escherichia coli
expression of beta2 subunit alone or in combination with other subunits in Escherichia coli
gene Prkab1, recombinant expression of GST-tagged subunit beta1 in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Riek, U.; Scholz, R.; Konarev, P.; Rufer, A.; Suter, M.; Nazabal, A.; Ringler, P.; Chami, M.; Mueller, S.A.; Neumann, D.; Forstner, M.; Hennig, M.; Zenobi, R.; Engel, A.; Svergun, D.; Schlattner, U.; Wallimann, T.
Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding
J. Biol. Chem.
283
18331-18343
2008
Rattus norvegicus (P54645), Rattus norvegicus (P80385), Rattus norvegicus (P80386), Rattus norvegicus (Q09137)
Manually annotated by BRENDA team
Mobbs, J.I.; Koay, A.; Di Paolo, A.; Bieri, M.; Petrie, E.J.; Gorman, M.A.; Doughty, L.; Parker, M.W.; Stapleton, D.I.; Griffin, M.D.; Gooley, P.R.
Determinants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinase
Biochem. J.
468
245-257
2015
Rattus norvegicus (P80386), Rattus norvegicus (Q9QZH4)
Manually annotated by BRENDA team