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Literature summary extracted from

  • Nandi, S.; Dey, M.
    Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2 (2020), J. Biol. Chem., 295, 5390-5403 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.40 L-asparagine
-
 Homo sapiens
2.7.1.40 L-aspartate
-
 Homo sapiens
2.7.1.40 L-serine
-
 Homo sapiens

Application

EC Number Application Comment Organism
2.7.1.40 drug development human pyruvate kinase muscle isoform 2 is considered an attractive therapeutic target for modulating tumor metabolism. Structure-function analyses of amino acid-mediated PKM2 regulation revealing the chemical requirements in the development of mechanism-based small-molecule modulators targeting the amino acid-binding pocket of PKM2 and provide broader insights into the regulatory mechanisms of complex allosteric enzyme Homo sapiens
2.7.1.40 medicine human pyruvate kinase muscle isoform 2 is considered an attractive therapeutic target for modulating tumor metabolism Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.40 L-cysteine
-
 Homo sapiens
2.7.1.40 L-valine
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.40 Homo sapiens A0A024R5Z9
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.40 carcinoma cell
-
 Homo sapiens
-
2.7.1.40 skeletal muscle
-
 Homo sapiens
-

Synonyms

EC Number Synonyms Comment Organism
2.7.1.40 PKM2
-
 Homo sapiens
2.7.1.40 pyruvate kinase muscle isoform 2
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.1.40 additional information amino acid-bound crystal structures of PKM2 display distinctive interactions within the binding pocket, causing unique allosteric effects in the enzyme. Structure-function analyses of amino acid-mediated PKM2 regulation, overview, revealing the chemical requirements in the development of mechanism-based small-molecule modulators targeting the amino acid-binding pocket of PKM2 and provide broader insights into the regulatory mechanisms of complex allosteric enzyme Homo sapiens
2.7.1.40 physiological function pyruvate kinase muscle isoform 2 (PKM2) is a key glycolytic enzyme involved in ATP generation and critical for cancer metabolism. PKM2 is expressed in many human cancers and is regulated by complex mechanisms that promote tumor growth and proliferation. Amino acids are involved in regulation of pyruvate kinase muscle isoform 2, overview. Various stimuli allosterically regulate PKM2 by cycling it between highly active and less active states. Several small molecules activate PKM2 by binding to its intersubunit interface. Despite binding similarly to PKM2, cysteine and serine differentially regulate the enzyme Homo sapiens