Target Name: PKM
NCBI ID: G5315
Other Name(s): Pyruvate kinase muscle isozyme | epididymis secretory protein Li 30 | P58 | Thyroid hormone-binding protein, cytosolic | Cytosolic thyroid hormone-binding protein | PKM variant 2 | PKM variant 4 | tumor M2-PK | Pyruvate kinase PKM | KPYM_HUMAN | Pyruvate kinase PKM (isoform c) | pyruvate kinase, muscle | pyruvate kinase M1/2 | pyruvate kinase muscle isozyme | pyruvate kinase isozymes M1/M2 | MGC3932 | Epididymis secretory protein Li 30 | Pyruvate kinase PKM (isoform a) | Tyrosine-protein kinase PKM2 | OIP-3 | PKM2 | Pyruvate kinase muscle | PK3 | OIP3 | Opa-interacting protein 3 | HEL-S-30 | threonine-protein kinase PKM2 | tyrosine-protein kinase PKM2 | thyroid hormone-binding protein 1 | thyroid hormone-binding protein, cytosolic | THBP1 | CTHBP | PKM variant 1 | Pyruvate kinase 2/3 | TCB | p58 | Pyruvate kinase PKM (isoform b) | Pyruvate kinase muscle isozym | Pyruvate kinase, muscle | OPA-interacting protein 3 | Pyruvate kinase isozymes M1/M2 | cytosolic thyroid hormone-binding protein | pyruvate kinase 2/3 | Pyruvate kinase M1/2 | Tumor M2-PK | PK, muscle type | Thyroid hormone-binding protein 1 | Threonine-protein kinase PKM2

PKM: Enzyme in Muscle Metabolism and Disease

PKM (Pyruvate Kinase Muscle Isozyme) is an enzyme that plays a crucial role in the metabolism of muscle growth and repair. It is a key enzyme in the muscle growth and repair process, and is often used as a drug target or biomarker in the study of muscle physiology and disease.

PKM is an enzyme that is found in muscle tissue and is responsible for the breakdown of pyruvate, a critical compound in muscle metabolism. Pyruvate is a key precursor to muscle protein synthesis and is essential for muscle growth and repair. The breakdown of pyruvate by PKM is regulated by several other enzymes, including the forkhead transcription factor (FHF1) and the muscle-specific protein kinase (Myk).

PKM has been shown to play a key role in the regulation of muscle growth and repair. Studies have shown that when PKM is expressed in muscle tissue, it is necessary for the growth and development of muscle tissue. In addition, PKM has been shown to play a key role in the regulation of muscle repair after injury.

PKM is also a potential drug target in the study of muscle physiology and disease. Several studies have shown that inhibiting PKM activity can lead to muscle growth and strength in individuals with muscle-related diseases. For example, a study published in the journal Nature Medicine used PKM as a drug target to treat muscle-related diseases, such as muscle dystrophy and myopathies. The study showed that inhibiting PKM activity in muscle tissue led to an improvement in muscle strength and function in the affected muscles.

In addition to its potential as a drug target, PKM is also a potential biomarker in the study of muscle physiology and disease. The breakdown of pyruvate by PKM has been shown to be affected by a variety of factors, including muscle fiber type, exercise intensity, and nutrient availability. Several studies have shown that the levels of PKM activity in muscle tissue can be used as a biomarker for muscle physiology and disease. For example, a study published in the journal Diabetes showed that PKM activity was significantly increased in muscle tissue from individuals with type 2 diabetes, and that this increase was associated with muscle dysfunction and decreased muscle mass.

PKM is also a key enzyme in the regulation of muscle metabolism, which is of great interest in the context of aging. As we age, muscle mass and function decline, and this is thought to be due to a variety of factors, including increased muscle breakdown and decreased muscle growth. The regulation of muscle metabolism by PKM is important for maintaining muscle mass and function in aging individuals.

In conclusion, PKM is an enzyme that plays a crucial role in the metabolism of muscle growth and repair. It is a potential drug target and biomarker in the study of muscle physiology and disease, and is of great interest in the context of aging. Further research is needed to fully understand the role of PKM in muscle physiology and disease.

Protein Name: Pyruvate Kinase M1/2

Functions: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:20847263, PubMed:15996096, PubMed:1854723). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:20847263, PubMed:15996096, PubMed:1854723). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:20847263, PubMed:15996096, PubMed:1854723)

More Common Targets

PKMP1 | PKMYT1 | PKN1 | PKN2 | PKN2-AS1 | PKN3 | PKNOX1 | PKNOX2 | PKNOX2-DT | PKP1 | PKP2 | PKP3 | PKP4 | PKP4-AS1 | PLA1A | PLA2G10 | PLA2G12A | PLA2G12AP1 | PLA2G12B | PLA2G15 | PLA2G1B | PLA2G2A | PLA2G2C | PLA2G2D | PLA2G2E | PLA2G2F | PLA2G3 | PLA2G4A | PLA2G4B | PLA2G4C | PLA2G4D | PLA2G4E | PLA2G4F | PLA2G5 | PLA2G6 | PLA2G7 | PLA2R1 | PLAA | PLAAT1 | PLAAT2 | PLAAT3 | PLAAT4 | PLAAT5 | PLAC1 | PLAC4 | PLAC8 | PLAC8L1 | PLAC9 | PLAC9P1 | PLAG1 | PLAGL1 | PLAGL2 | Plasma Membrane Calcium ATPase | PLAT | Platelet Glycoprotein Ib Complex | Platelet-activating factor acetylhydrolase isoform 1B complex | Platelet-Derived Growth Factor (PDGF) | Platelet-Derived Growth Factor Receptor | PLAU | PLAUR | PLB1 | PLBD1 | PLBD1-AS1 | PLBD2 | PLCB1 | PLCB2 | PLCB3 | PLCB4 | PLCD1 | PLCD3 | PLCD4 | PLCE1 | PLCE1-AS2 | PLCG1 | PLCG1-AS1 | PLCG2 | PLCH1 | PLCH2 | PLCL1 | PLCL2 | PLCXD1 | PLCXD2 | PLCXD3 | PLCZ1 | PLD1 | PLD2 | PLD3 | PLD4 | PLD5 | PLD6 | PLEC | PLEK | PLEK2 | PLEKHA1 | PLEKHA2 | PLEKHA3 | PLEKHA4 | PLEKHA5 | PLEKHA6 | PLEKHA7