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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: Q9QZH4
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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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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
subunit AMPKbeta-2
UniProt
Manually annotated by BRENDA team
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?
AAKB2_RAT
271
0
30227
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
AMPK is heterotrimer with alphabetagamma structure
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified subunit beta2 carbohydrate-binding module, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 13 mg/ml protein in 20 mM HEPES, pH 7.0, with or without 6 mM glucosyl-beta-cyclodextrin, with 0.001 ml of reservoir solution, which contains for the unliganded enzyme 0.17 M ammonium sulfate, 15% v/v glycerol and 25.5% w/v PEG 4000, or contains 0.2 M lithium chloride, 20% w/v PEG 6000 and 0.1 M sodium HEPES, pH 7.0 for the complex with gBCD, X-ray diffraction structure determination and analysis at 1.6-2.0 A reolution, 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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Prkab2, recombinant expression of GST-tagged subunit beta2 in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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