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Literature summary for 2.7.11.31 extracted from

  • Yu, D.; Peng, Y.; Ayaz-Guner, S.; Gregorich, Z.R.; Ge, Y.
    Comprehensive characterization of AMP-activated protein kinase catalytic domain by top-down mass spectrometry (2016), J. Am. Soc. Mass Spectrom., 27, 220-232.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information activation of the enzyme by phosphorylation Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged AMPK catalytic domain in Escherichia coli strain Rossetta (DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information C-terminal truncation of AMPKalpha at residue 312 yields a protein that is active upon phosphorylation of Thr172 in the absence of beta and gamma subunits, which is refered to as the AMPK catalytic domain and commonly used to substitute for AMPK heterotrimeric complex in in vitro kinase assays Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13131
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein activation of the enzyme by phosphorylation of Thr172 of the alpha subunit. Thr172 is the only site phosphorylated by its upstream kinase, liver kinase B1, and the phosphorylation dramatically increases the kinase activity of the catalytic domain/alpha-subunit. Phosphorylation of AMPK alpha1 on Thr172 by LKB1/Ste20-related adaptor (STRAD)/mouse protein 25(MO25) complex. Top-down mass spectrometric analysis, overview. Ser18 and Ser22 in the His-tag region as well as Thr196 (equivalent to Thr172 in the unmodified enzyme) in the sequence of the AMPK catalytic domain are the three phosphorylation sites Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin-GGHMRSAMSGLHLVKRR-NH2 i.e. SAMS peptide, a peptide derived from residues 73-85 of rat acetyl-CoA carboxylase in which Ser77 is mutated to Ala and the AMPK phosphorylation site is Ser79 Homo sapiens ADP + phosphorylated biotin-GGHMRSAMpSGLHLVKRR-NH2
-
?

Subunits

Subunits Comment Organism
? x * 37953, recombinant phosphorylated AMPK alpha1 subunit, mass spectrometry Homo sapiens
heterotrimer enzyme AMPK is a heterotrimeric protein complex composed of a catalytic subunit (alpha) and two regulatory subunits (beta and gamma) Homo sapiens

Synonyms

Synonyms Comment Organism
AMP-activated protein kinase
-
Homo sapiens
AMPK
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
AMP
-
Homo sapiens

General Information

General Information Comment Organism
physiological function AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that is essential in regulating energy metabolism in all eukaryotic cells Homo sapiens