glycolytic enzyme

Pathways Recommended:	Metabolic Enzyme/Protease

By Targets:	Endogenous Metabolite (6) Keap1-Nrf2 (1) Phosphatase (1)
By Research Areas:	Cancer (2) Endocrinology (1) Infection (1) Metabolic Disease (4) Neurological Disease (1)

Targets Recommended: Angiotensin-converting Enzyme (ACE) NEDD8-activating Enzyme E1/E2/E3 Enzyme IRE1 TET Protein

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-P2726

Aldolase, Rabbit muscle Fructose-diphosphate aldolase	Endogenous Metabolite	Metabolic Disease
Aldolase, Rabbit muscle is a glycolytic enzyme and a component of the VATPase complex. Aldolase causes fructose 1, 6-diphosphate to decompose into dihydroxyacetone and glyceraldehyde 3-phosphate .

HY-P2776

Hexokinase, microorganism	Endogenous Metabolite	Metabolic Disease
Hexokinase (ScHEX1) (EC 2.7.1.1) is a glycolytic enzyme hexokinase that is inhibited by n-acetylglucosamine. Inhibition of Hexokinase (ScHEX1) by n-acetylglucosamine leads to its separation from the mitochondrial outer membrane, resulting in activation of NLRP3 inflammasome .

HY-138877A

Phosphoglycolic acid lithium	Phosphatase	Cancer
Phosphoglycolic acid (lithium) is a competitive inhibitor of phosphoglycerate mutase (PGAM)-B, an enzyme of the glycolytic pathway. Phosphoglycolic acid increases basal and fMLF-induced levels of G6P in intact neutrophils. Phosphoglycolic acid thereby increases upstream intermediates in neutrophils, thereby amplifying the respiratory oxidative burst .

HY-P2931

Triosephosphate isomerase TPI	Endogenous Metabolite	Others
Triosephosphate isomerase (TPI) is a glycolytic enzyme. Triosephosphate isomerase fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate, its catalytic site is at the dimer interface .

HY-P2806

Pyruvate Kinase, Microorganism PK; Fluorokinase	Endogenous Metabolite	Metabolic Disease
Pyruvate Kinase, Microorganism (PK) is a glycolytic enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP .

HY-P2918

Phosphoglucose Isomerase, Baker's yeast (S. cerevisiae) GPI; Phosphoglucose Isomerase	Endogenous Metabolite	Others
Phosphoglucose Isomerase, Baker's yeast (S. cerevisiae) (GPI), i.e., phosphoglucose isomerase/phosphoglucoisomerase (PGI) or phosphohexose isomerase (PHI), is often used in biochemical studies. Glucose 6-phosphate isomeras is a highly conserved glycolytic and dimeric enzyme. Glucose 6-phosphate isomeras catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate .

HY-134205A

CBR-470-1 1 Publications Verification	Keap1-Nrf2	Neurological Disease Metabolic Disease
CBR-470-1 is an inhibitor of the glycolytic enzyme phosphoglycerate kinase 1 (PGK1). CBR-470-1 is also a non-covalent Nrf2 activator. CBR-470-1 protects SH-SY5Y neuronal cells against MPP ⁺-induced cytotoxicity through activation of the Keap1-Nrf2 cascade .

HY-P2822

Phosphoglycerate kinase, yeast PGK	Endogenous Metabolite	Infection Endocrinology Cancer
Phosphoglycerate kinase, yeast (PGK), namely phosphoglycerate kinase, is a glycolytic enzyme commonly used in biochemical research. Phosphoglycerate kinase can catalyze the reversible transfer of phosphate groups from 1,3-bisphosphoglycerate (1,3-BPG) to ADP to generate 3-phosphoglycerate (3-PG) and ATP. At the same time, it can also participate in gluconeogenesis, catalyzing the opposite reaction to produce 1,3BPGA and ADP. Phosphoglycerate kinase is involved in energy metabolism, interaction with nucleic acid, tumor progression, cell death and virus replication and other related processes .

Cat. No.	Product Name

HY-L058

Glycolysis Compound Library	689 compounds
Glycolysis is a series of metabolic processes by which one molecule of glucose is catabolized to two molecules of pyruvate with a net gain of two ATP. Glycolysis takes place in 10 steps and catalyzed by a series of enzyme, such as hexokinase, Glucose-6-phosphate isomerase, Phosphofructokinase, etc. Glycolysis is used by all cells in the body for energy generation. Most cancer cells exhibit increased glycolysis and use this metabolic pathway for generation of ATP as a main source of their energy supply. This phenomenon is known as the Warburg effect and is considered as one of the most fundamental metabolic alterations during malignant transformation. Because increased aerobic glycolysis is commonly seen in a wide spectrum of human cancers, development of novel glycolytic inhibitors as a new class of anticancer agents is likely to have broad therapeutic applications. MCE provides a unique collection of 689 glycolysis compounds that mainly target hexokinase, glucokinase, enolase, pyruvate kinase, PDHK, etc. MCE Glycolysis Compound Library is a useful tool for glucose metabolism research and anti-cancer drug discovery.

Glycolysis Compound Library

689 compounds

Glycolysis is a series of metabolic processes by which one molecule of glucose is catabolized to two molecules of pyruvate with a net gain of two ATP. Glycolysis takes place in 10 steps and catalyzed by a series of enzyme, such as hexokinase, Glucose-6-phosphate isomerase, Phosphofructokinase, etc. Glycolysis is used by all cells in the body for energy generation.

Most cancer cells exhibit increased glycolysis and use this metabolic pathway for generation of ATP as a main source of their energy supply. This phenomenon is known as the Warburg effect and is considered as one of the most fundamental metabolic alterations during malignant transformation. Because increased aerobic glycolysis is commonly seen in a wide spectrum of human cancers, development of novel glycolytic inhibitors as a new class of anticancer agents is likely to have broad therapeutic applications.

MCE provides a unique collection of 689 glycolysis compounds that mainly target hexokinase, glucokinase, enolase, pyruvate kinase, PDHK, etc. MCE Glycolysis Compound Library is a useful tool for glucose metabolism research and anti-cancer drug discovery.

Cat. No.	Product Name	Type

HY-P2931

Triosephosphate isomerase TPI	Biochemical Assay Reagents
Triosephosphate isomerase (TPI) is a glycolytic enzyme. Triosephosphate isomerase fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate, its catalytic site is at the dimer interface .

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