Literature summary for 2.7.11.31 extracted from

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 (2015), Biochem. J., 468, 245-257.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene Prkab1, recombinant expression of GST-tagged subunit beta1 in Escherichia coli strain BL21(DE3)	Rattus norvegicus
gene Prkab2, recombinant expression of GST-tagged subunit beta2 in Escherichia coli strain BL21(DE3)	Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Rattus norvegicus
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	Rattus norvegicus

Crystallization (Comment)

Organism

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

Rattus norvegicus

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

Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	glucosyl-beta-cyclodextrin binding kinetics, association and dissociation, and thermodynamics	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P80386	subunit AMPKbeta-1	-
Rattus norvegicus	Q9QZH4	subunit AMPKbeta-2	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged subunit beta1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, anion exchange chromatography, and ultrafiltration	Rattus norvegicus

Subunits

Subunits	Comment	Organism
heterotrimer	AMPK is heterotrimer with alphabetagamma structure	Rattus norvegicus
More	the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM). The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, determination of the NMR solution structure, structure analysis	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
AMP-activated protein kinase	-	Rattus norvegicus
AMPK	-	Rattus norvegicus
AMPKbeta-1	-	Rattus norvegicus
AMPKbeta-2	-	Rattus norvegicus

General Information

General Information	Comment	Organism
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	Rattus norvegicus
additional information	the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter	Rattus norvegicus