Coenzyme A and Its Derivatives: From a Metabolic Hub to Multidisease Regulation
Coenzyme A and Its Derivatives: From a Metabolic Hub to Multidisease Regulation
Coenzyme A (CoA) is an essential intracellular acyl-group carrier. By combining with different acyl groups, CoA forms various acyl-CoAs that connect carbohydrate, lipid, and amino acid metabolism. Through carbon-flux distribution, CoA-pool balance, and protein acylation, CoA and its derivatives participate in the regulation of multiple diseases.
Keywords: coenzyme A; CoA; acetyl-CoA; malonyl-CoA; succinyl-CoA; propionyl-CoA; protein acylation; metabolic reprogramming; disease regulation
1 Metabolic Basis of CoA and Its Derivatives
1.1 CoA as an Intracellular Acyl-Group Carrier
CoA participates extensively in cellular carbon metabolism. Its terminal thiol group forms thioester bonds with different acyl groups, producing acetyl-CoA, malonyl-CoA, succinyl-CoA, propionyl-CoA, and other acyl-CoAs.
The acyl group determines the principal metabolic direction of each derivative. Acetyl-CoA can enter the tricarboxylic acid cycle or support lipid synthesis, malonyl-CoA participates in de novo fatty acid synthesis, succinyl-CoA connects the TCA cycle with heme biosynthesis, and propionyl-CoA participates in the processing of carbon derived from certain amino acids, odd-chain fatty acids, and propionate.
1.2 CoA Biosynthesis and Metabolic-Pool Balance
(1) De Novo CoA Biosynthesis
CoA is synthesized through a multistep enzymatic pathway using pantothenate (vitamin B5), cysteine, ATP, and other substrates. Pantothenate kinase (PANK) catalyzes the initial step and is an important regulatory node controlling CoA biosynthetic flux.
Subsequent reactions introduce cysteine, mediate decarboxylation, and construct the nucleotide portion of CoA. CoA synthase (COASY) catalyzes the final two steps, ultimately generating CoA.
(2) Balance Between Free CoA and Acyl-CoA
Intracellular CoA exists both in a free form and in acylated forms. Free CoA continuously participates in pyruvate oxidation, fatty acid β-oxidation, and acyl-group activation. CoA is subsequently released when acyl-CoAs enter downstream reactions.
Excessive accumulation of a particular acyl-CoA can reduce the available free CoA pool and restrict other CoA-dependent reactions.
1.3 Subcellular Compartmentalization of CoA Metabolism
(1) Mitochondrial CoA Pools
Mitochondrial CoA primarily participates in pyruvate oxidation, the TCA cycle, fatty acid β-oxidation, and the degradation of certain amino acids. Acetyl-CoA, succinyl-CoA, propionyl-CoA, and fatty acyl-CoAs of different chain lengths can all be formed or converted within the mitochondrial metabolic network.
(2) Cytosolic and Nuclear CoA Pools
Cytosolic acetyl-CoA primarily supports the synthesis of fatty acids, cholesterol, and other lipids. Malonyl-CoA is an important substrate for de novo fatty acid synthesis. In the nucleus, localized acetyl-CoA generation and utilization help sustain protein acetylation.
Carbon sources and acyl groups can be redistributed among compartments through citrate, acetate, acylcarnitines, and related metabolites.
1.4 Major CoA Derivatives and Their Functions
CoA or Derivative | Major Source or Formation Route | Principal Metabolic Function | Major Regulatory Direction |
CoA | Pantothenate-dependent de novo biosynthesis | Common cofactor for acyl transfer | Free CoA pool and overall acyl metabolism |
Acetyl-CoA | Pyruvate, fatty acids, certain amino acids, and acetate | TCA cycle and fatty acid and cholesterol synthesis | Protein acetylation and carbon-flux distribution |
Malonyl-CoA | Carboxylation of acetyl-CoA by ACC | De novo fatty acid synthesis | CPT1 regulation and fatty acid oxidation |
Succinyl-CoA | α-Ketoglutarate and downstream metabolism of propionyl-CoA | TCA cycle and heme biosynthesis | Protein succinylation |
Propionyl-CoA | Certain amino acids, odd-chain fatty acids, and propionate | Conversion into succinyl-CoA | Organic acid metabolism and CoA-pool balance |
Acetoacetyl-CoA | Condensation of acetyl-CoA and related reactions | Ketone-body- and cholesterol-associated metabolism | Distribution of acetyl-derived carbon |
Long-chain acyl-CoA | Activation of long-chain fatty acids | β-Oxidation and glycerolipid and membrane-lipid synthesis | Substrate selection and lipid distribution |
2 How Major CoA Derivatives Regulate Cellular Metabolism
2.1 Acetyl-CoA Connects Energy Production with Anabolism
(1) Mitochondrial Acetyl-CoA and Energy Production
Pyruvate generated through glycolysis can be converted into acetyl-CoA by the pyruvate dehydrogenase complex. Fatty acid β-oxidation and the degradation of certain amino acids also generate acetyl-CoA.
Within mitochondria, acetyl-CoA condenses with oxaloacetate to form citrate and enter the TCA cycle. This process generates reducing equivalents such as NADH and FADH₂, which support oxidative phosphorylation and ATP production.
(2) Cytosolic Acetyl-CoA and Anabolism
Citrate generated in mitochondria can be exported to the cytosol, where ATP citrate lyase (ACLY) converts it back into acetyl-CoA. Acetyl-CoA synthetase 2 (ACSS2) can also generate acetyl-CoA from acetate.
Cytosolic acetyl-CoA provides an important carbon source for the synthesis of fatty acids, cholesterol, and other acetyl-group-dependent biomolecules.
2.2 Malonyl-CoA Controls Fatty Acid Synthesis and Oxidation
(1) Two-Carbon Donor for Fatty Acid Synthesis
Malonyl-CoA is generated through the acetyl-CoA carboxylase (ACC)-catalyzed carboxylation of acetyl-CoA. It serves as an essential two-carbon donor during de novo fatty acid synthesis and participates in fatty acid-chain elongation through sequential condensation and reduction reactions catalyzed by fatty acid synthase.
(2) CPT1 and Fatty Acid β-Oxidation
Malonyl-CoA inhibits carnitine palmitoyltransferase 1 (CPT1), thereby reducing the entry of long-chain fatty acyl groups into mitochondria. Increased malonyl-CoA suppresses CPT1 and decreases mitochondrial fatty acid import, whereas reduced malonyl-CoA weakens this inhibition.
Acetyl-CoA → ACC → Malonyl-CoA → Increased fatty acid synthesis
Malonyl-CoA ┤ CPT1 → Reduced mitochondrial entry of long-chain fatty acids → Reduced β-oxidation
2.3 Succinyl-CoA Connects the TCA Cycle with Heme Biosynthesis
Succinyl-CoA is primarily generated from α-ketoglutarate by the α-ketoglutarate dehydrogenase complex. It can also be replenished from propionyl-CoA through the methylmalonyl-CoA pathway.
Within the TCA cycle, succinyl-CoA is converted into succinate in a reaction coupled to substrate-level phosphorylation. Succinyl-CoA can also combine with glycine in the initial reaction of heme biosynthesis.
2.4 Propionyl-CoA Connects Amino Acid Metabolism with the TCA Cycle
(1) Formation of Propionyl-CoA
Propionyl-CoA is generated through the degradation of amino acids such as valine, isoleucine, methionine, and threonine. It can also arise from odd-chain fatty acids and propionate metabolism.
(2) Conversion into Succinyl-CoA
Propionyl-CoA carboxylase (PCC) converts propionyl-CoA into methylmalonyl-CoA. Methylmalonyl-CoA mutase subsequently generates succinyl-CoA, which enters the TCA cycle.
When PCC or downstream metabolic steps are impaired, propionyl-CoA and associated organic acids can accumulate abnormally.
2.5 Long-Chain Acyl-CoAs Determine Fatty Acid Fate
After entering cells, long-chain fatty acids must first be activated into long-chain acyl-CoAs. These molecules can subsequently enter mitochondrial β-oxidation or be used to synthesize triglycerides, phospholipids, and other complex lipids.
When fatty acid uptake, storage, and oxidation become imbalanced, long-chain acyl-CoAs and their downstream lipid intermediates can accumulate.
3 CoA Derivatives in Protein Modification and Cellular Regulation
3.1 Acetyl-CoA and Protein Acetylation
(1) Histone Acetylation
Lysine acetyltransferases use acetyl-CoA as the acetyl-group donor and transfer acetyl groups to lysine residues on histones. Histone acetylation alters chromatin structure and the binding of regulatory proteins, thereby influencing gene transcription.
Acetyl-CoA-generating pathways involving ACLY, ACSS2, and related enzymes can affect this process by altering local acetyl-group availability.
(2) Non-Histone Protein Acetylation
Transcription factors, metabolic enzymes, cytoskeletal proteins, and numerous signaling proteins can also undergo lysine acetylation. Acetylation can alter protein stability, catalytic activity, subcellular localization, or protein–protein interactions.
3.2 Different Acyl-CoAs Support Distinct Protein Acylations
(1) Succinylation
Succinyl-CoA can provide succinyl groups for lysine succinylation. Many mitochondrial enzymes involved in the TCA cycle, fatty acid oxidation, and amino acid metabolism undergo succinylation. Some of these modifications are influenced by local succinyl-CoA concentrations and chemical reactivity.
SIRT5 possesses strong desuccinylase activity and can regulate the succinylation state of associated proteins.
(2) Malonylation and Propionylation
Malonyl-CoA and propionyl-CoA are associated with lysine malonylation and propionylation, respectively. Because these acyl groups differ in size, charge, and chemical properties, they can produce distinct structural and functional changes in modified proteins.
3.3 Competition Within the CoA Pool and CoA Trapping
Different intracellular acyl-CoAs share a limited CoA pool. Under normal conditions, acyl groups enter downstream metabolism and release CoA. When a particular acyl group cannot be cleared efficiently, substantial amounts of CoA may become trapped in the corresponding acyl-CoA form.
The resulting reduction in free CoA can restrict pyruvate oxidation, fatty acid β-oxidation, and other CoA-dependent reactions.
3.4 CoAlation and Oxidative Stress
Under oxidative stress, the thiol group of CoA can form reversible mixed disulfide bonds with cysteine residues in selected proteins, a modification known as protein CoAlation.
CoAlation can alter protein activity and protect sensitive cysteine residues from further irreversible oxidation. When oxidative stress subsides, CoAlation can be reversed.
4 CoA and Its Derivatives in Disease
4.1 Cancer: Acetyl-CoA and Metabolic Reprogramming
(1) Acetyl-CoA Supply and Lipid Synthesis
Rapidly proliferating tumor cells require continuous membrane-lipid synthesis. ACLY generates cytosolic acetyl-CoA from citrate, allowing glucose and other carbon sources to enter fatty acid and cholesterol synthesis. ACSS2 generates acetyl-CoA from acetate and can supplement the acetyl-group supply in certain hypoxic or nutrient-limited environments.
Increased acetyl-CoA availability can support the synthesis of membrane lipids and other biomolecules.
(2) Acyl-CoAs and Epigenetic Regulation
Changes in acetyl-CoA levels can alter histone and non-histone protein acetylation, enabling nutrient status and carbon-source utilization to influence tumor-associated transcriptional programs.
Changes in succinyl-CoA and protein succinylation can also regulate certain enzymes involved in glycolysis, the TCA cycle, and amino acid metabolism, creating reciprocal regulation between metabolic enzyme activity and acyl-CoA composition.
4.2 Obesity, Insulin Resistance, and MASLD
(1) Malonyl-CoA and Impaired Fatty Acid Utilization
Nutrient excess can alter malonyl-CoA production and fatty acid utilization. Through inhibition of CPT1, malonyl-CoA restricts the entry of long-chain fatty acids into mitochondria.
When fatty acid supply continuously exceeds oxidative and safe storage capacities, long-chain acyl-CoAs, diacylglycerols, and other lipid intermediates can accumulate. Increased diacylglycerol and related lipid signals can interfere with signaling downstream of the insulin receptor and contribute to insulin resistance.
(2) Acetyl-CoA and Redistribution of Hepatic Carbon Flux
Increased mitochondrial acetyl-CoA in the liver can promote pyruvate carboxylation and gluconeogenesis-associated processes, whereas cytosolic acetyl-CoA provides carbon for fatty acid and cholesterol synthesis.
During obesity and insulin resistance, redistribution of carbon flux among fatty acid uptake, β-oxidation, gluconeogenesis, and lipid synthesis can contribute to metabolic dysfunction-associated steatotic liver disease (MASLD) and metabolic abnormalities associated with type 2 diabetes.
4.3 Cardiovascular Disease: Acyl-CoAs and Myocardial Metabolic Flexibility
(1) Altered Myocardial Substrate Selection
The normal myocardium can use fatty acids, glucose, lactate, ketone bodies, and other substrates and adjust their relative contributions according to oxygen availability, nutritional state, and cardiac workload.
Malonyl-CoA regulates mitochondrial fatty acid entry through CPT1, whereas long-chain acyl-CoAs lie at the branch point between fatty acid oxidation and complex lipid synthesis. Fatty acid uptake and utilization are frequently increased in diabetic cardiomyopathy, whereas some forms of heart failure are accompanied by reduced fatty acid oxidation and impaired overall mitochondrial oxidative capacity. Both conditions can reduce myocardial metabolic flexibility.
(2) Lipid Intermediates and Mitochondrial Burden
When fatty acid supply exceeds myocardial oxidative capacity, long-chain acyl-CoAs can be redirected into lipid intermediates such as diacylglycerols and ceramides. These lipids can interfere with insulin signaling, membrane-associated signaling, and cell-survival pathways.
Accumulation of certain acylcarnitines is often associated with a mismatch between fatty acid β-oxidation and the oxidative capacity of the TCA cycle and respiratory chain. Persistent accumulation of lipid intermediates can increase mitochondrial metabolic stress and impair myocardial contractile function.
4.4 Neurodegenerative Disease: Defects in CoA Biosynthesis
(1) PANK2 and PKAN
PANK2 participates in the initial stage of de novo CoA biosynthesis. Pathogenic PANK2 variants can cause pantothenate kinase-associated neurodegeneration (PKAN).
PANK2 dysfunction can disrupt CoA availability and consequently affect fatty acyl metabolism, mitochondrial energy conversion, and membrane-lipid homeostasis. It is also associated with oxidative stress and characteristic brain iron accumulation. The precise connection between CoA metabolic abnormalities and iron-homeostasis disruption remains under investigation.
(2) COASY and CoPAN
COASY participates in the final steps of CoA biosynthesis. Pathogenic COASY variants can cause COASY protein-associated neurodegeneration (CoPAN) and related neurodegenerative phenotypes.
Restricted CoA generation can simultaneously impair mitochondrial oxidation, fatty acid and membrane-lipid metabolism, and protein acylation. Because neurons depend extensively on mitochondrial energy production and membrane-lipid renewal, sustained impairment of CoA supply can compromise both energy metabolism and membrane maintenance.
4.5 Propionyl-CoA and Inherited Organic Acidemias
(1) Abnormal Propionyl-CoA Accumulation
In propionic acidemia, PCC deficiency prevents propionyl-CoA from entering the methylmalonyl-CoA pathway normally. Accumulation of propionyl-CoA, 2-methylcitrate, and other abnormal metabolites can disrupt the TCA cycle, mitochondrial respiration, the urea cycle, and other metabolic processes.
(2) CoA Trapping and Systemic Metabolic Dysfunction
When large amounts of propionyl-CoA accumulate, CoA remains sequestered in an abnormal acylated form, reducing the availability of free CoA. Pyruvate oxidation, fatty acid oxidation, and other CoA-dependent processes can consequently become restricted.
These metabolic abnormalities may be accompanied by metabolic acidosis, neurological injury, cardiomyopathy, and recurrent episodes of metabolic decompensation.
5 Disease-Intervention Strategies Targeting CoA Metabolism
5.1 Restoring CoA Availability and the Free CoA Pool
(1) CoA Biosynthesis Defects
Strategies targeting abnormalities in PANK2, COASY, and other CoA biosynthetic nodes primarily focus on supplementing CoA-related precursors, bypassing selected blocked steps, and increasing residual CoA-generating capacity.
Because different genetic defects affect different stages of the biosynthetic pathway, the available metabolic bypasses also differ.
(2) Clearance of Abnormal Acyl-CoAs
For CoA trapping caused by the accumulation of abnormal acyl groups such as propionyl-CoA, reducing precursor load, limiting abnormal acyl-CoA formation, or promoting alternative clearance can decrease CoA sequestration and improve free CoA availability.
5.2 Restricting Abnormal Acetyl-CoA Supply
(1) Targeting ACLY
ACLY inhibition can reduce the supply of citrate-derived cytosolic acetyl-CoA and suppress fatty acid and cholesterol synthesis. This strategy can be used to investigate tumor-cell dependence on cytosolic acetyl-CoA and interventions targeting abnormal lipid metabolism.
(2) Targeting ACSS2
ACSS2 inhibition restricts acetate-derived acetyl-CoA production and reduces alternative acetyl-group supply in cells dependent on acetate utilization or adaptation to nutrient stress.
ACSS2 and ACLY therefore represent different carbon-source entry points into the acetyl-CoA pool.
5.3 Regulating Malonyl-CoA and Fatty Acid Utilization
(1) ACC and MCD Regulation
ACC controls malonyl-CoA generation, whereas malonyl-CoA decarboxylase (MCD) participates in its degradation. Regulating these enzymes can simultaneously alter de novo fatty acid synthesis and CPT1-mediated mitochondrial fatty acid import.
(2) Tissue-Specific Metabolic Effects
The liver possesses substantial lipid-synthetic capacity, whereas the myocardium and skeletal muscle rely more strongly on fatty acid oxidation for energy production. Intervention in the ACC–malonyl-CoA–CPT1 axis must therefore account for tissue-specific substrate requirements and oxidative capacity.
5.4 Regulating Acyl-CoA-Dependent Protein Acylation
(1) Altering Acyl-Group Donor Availability
Changing the availability of acetyl-CoA, succinyl-CoA, and other acyl-group donors can alter corresponding protein-acylation levels while simultaneously affecting lipid synthesis, the TCA cycle, and other metabolic processes.
(2) Targeting Acylation and Deacylation Enzymes
Lysine acetyltransferases, histone deacetylases (HDACs), and members of the sirtuin family directly regulate protein-acylation states. SIRT5 possesses strong desuccinylase, demalonylase, and deglutarylase activities and can be used to regulate or characterize protein modifications associated with changes in mitochondrial acyl-CoAs.
6 Products
6.1 Products for CoA and Major Acyl-CoA Research
Catalog # | Product Name | Grade and Purity | Mechanism and Research Application |
Coenzyme A hydrate (free acid) | ≥85%(HPLC) | The terminal thiol accepts and transfers different acyl groups; used as a foundational cofactor in CoA-dependent enzymatic reactions and in studies of free CoA utilization, acyl activation, and acyl transfer | |
Coenzyme A (sodium salt hydrate ) | ≥95% | Provides CoA for acyl-transfer reactions; used to establish CoA-dependent enzymatic systems and analyze conversion between free CoA and different acyl-CoAs | |
Acetyl-Coenzyme A trilithium salt | 85% (Enzymatic and Absorbance), 2% (lithium) | High-energy acetyl-group donor and direct substrate for multiple enzymes; used in acetyl-transfer reactions, TCA-cycle-associated enzymatic assays, and protein-acetylation systems | |
Acetyl coenzyme A sodium salt | ≥90% | Provides acetyl groups for metabolic and protein-modification reactions; used in lipid synthesis, metabolic enzyme reactions, and protein-acetylation research | |
Acetyl Coenzyme A (Acetyl-CoA) Assay Kit (UV Micro Method) | BioReagent | Uses a UV microassay to quantify acetyl-CoA-associated reaction signals; used to compare changes in acetyl-CoA metabolic pools under different treatment conditions | |
Malonyl coenzyme A tetralithium salt | ≥90% | Serves as a two-carbon donor in fatty acid synthesis and as a substrate for related enzymes; used to investigate fatty acid synthesis, malonyl-CoA utilization, and enzyme kinetics | |
Malonyl coenzyme A lithium salt | ≥90%(HPLC) | Malonyl-group donor and metabolic substrate; used to analyze malonyl-CoA-dependent fatty acid synthesis and related enzymatic processes | |
Malonyl-¹³C₃ coenzyme A lithium salt | ≥99 atom% ¹³C, ≥95% | Provides a traceable ¹³C-labeled malonyl carbon source; used for downstream malonyl-CoA carbon-flux tracing, metabolite identification, and quantitative analysis | |
propionyl-CoA | Moligand™ | Serves as a propionyl-group donor and an intermediate in organic acid metabolism; used to study propionyl-CoA metabolism, CoA trapping, and conversion to methylmalonyl-CoA. | |
methylmalonyl-CoA | Moligand™ | Intermediate in the conversion of propionyl-CoA to succinyl-CoA; used to investigate methylmalonyl-CoA metabolism and anaplerotic entry into the TCA cycle. | |
Succinyl coenzyme A sodium salt | ≥85% | TCA-cycle intermediate and succinyl-group source; used in succinyl-CoA-dependent enzymatic reactions, heme-associated metabolism, and protein-succinylation research | |
Acetoacetyl coenzyme A sodium salt hydrate | ≥90% | Serves as an acetoacetyl-CoA substrate and an acetyl-derived carbon intermediate; used to study ketone-body- and cholesterol-associated metabolism and acetyl-derived carbon allocation. | |
stearoyl-CoA | 92-98% | Representative saturated long-chain acyl-CoA; used to study metabolic partitioning of activated long-chain fatty acids among β-oxidation, glycerolipid synthesis, and membrane-lipid synthesis. |
6.2 Products for Acetyl-CoA Generation and Fatty Acid Metabolism
Catalog # | Product Name | Grade and Purity | Mechanism and Research Application |
Pyruvate Dehydrogenase (PDH) Activity Assay Kit (DCPIP, Micro Method) | BioReagent | Uses DCPIP-associated signal changes to evaluate PDH catalytic capacity; used to analyze the ability of pyruvate to enter the acetyl-CoA metabolic pathway | |
ATP Citrate Lyase (ACL) Activity Assay Kit (UV Micro Method) | BioReagent | Evaluates ACL-catalyzed reactions using a UV microassay; used to analyze the capacity for citrate-derived cytosolic acetyl-CoA production | |
ATP Citrate Lyase (ACL) Activity Assay Kit (UV Colorimetric Method) | BioReagent | Evaluates ACL activity through catalytic absorbance changes; used to compare citrate cleavage and acetyl-CoA generation under different conditions | |
BMS 303141 | ≥98% | Inhibits ACLY-mediated citrate cleavage and reduces cytosolic acetyl-CoA availability; used to investigate the dependence of lipid synthesis and protein acetylation on the ACLY pathway | |
SB 204990 | ≥98%(HPLC) | Interferes with ACLY catalytic activity and reduces citrate-derived acetyl-CoA; used to characterize the role of ACLY in lipid synthesis and metabolic reprogramming | |
ACSS2 Human Pre-designed siRNA Set A | — | Downregulates ACSS2 through RNA interference; used to verify ACSS2 dependency in acetate reutilization and acetate-derived acetyl-CoA production | |
ACSS2-IN-1 | — | Pharmacologically interferes with ACSS2 function and reduces acetate activation; used to investigate acetate utilization and alternative acetyl-CoA supply | |
Recombinant ACSS2 Antibody | KD Validation | Specifically detects ACSS2 protein; used to verify genetic interventions and analyze relationships between ACSS2 changes and acetate-utilization phenotypes | |
Acetyl CoA Carboxylase (ACC) Activity Assay Kit (AHM, Micro Method) | BioReagent | Uses an AHM-based microassay to evaluate ACC catalytic activity; used to analyze the allocation of acetyl-CoA toward malonyl-CoA and the state of fatty acid synthesis | |
Acetyl-CoA Carboxylase (ACC) Activity Assay Kit (AHM, Colorimetric Method) | BioReagent | Uses an AHM-based colorimetric assay to evaluate ACC catalytic capacity; used to compare malonyl-CoA generation and fatty acid synthesis under different conditions | |
PF 05175157 | ≥98%(HPLC) | Inhibits ACC1/2 and reduces carboxylation flux from acetyl-CoA to malonyl-CoA; used to study the ACC–malonyl-CoA–CPT1 axis and the balance between fatty acid synthesis and oxidation. | |
Acetyl-CoA Carboxylase-IN-1 | Moligand™, 10 mM in DMSO | Pre-prepared ACC inhibitor solution; used for pharmacological ACC inhibition and dose–response studies and to analyze changes in malonyl-CoA generation and fatty acid metabolism. | |
Human Acetyl Coenzyme A Carboxylase Alpha (ACACa) ELISA Kit | BioReagent | Quantifies ACACA protein by ELISA; used to analyze the relationship between ACACA abundance and fatty acid-synthesis phenotypes | |
Acyl-CoA Synthetase (ACS) | Bioactive, Recombinant, ActiBioPure™, High Performance, EnzymoPure™, ≥90%(SDS-PAGE), ≥4 U/mg enzyme powder; ≥30 U/mg protein | Catalyzes formation of acyl-CoA from fatty acids and CoA; used to study fatty acid activation, acyl-CoA generation, and fatty acid metabolic flux. | |
Carnitine Palmitoyltransferase Activity Assay Kit (Micro Method) | BioReagent | Evaluates carnitine palmitoyltransferase activity through an associated enzymatic reaction; used to analyze mitochondrial entry of long-chain fatty acyl groups and fatty acid oxidation | |
Carnitine Palmitoyltransferase Activity Assay Kit (Colorimetric Method) | BioReagent | Evaluates carnitine palmitoyltransferase activity through a colorimetric enzymatic signal; used to investigate mitochondrial fatty acid entry and substrate utilization |
6.3 Products for Protein Acylation Research
Catalog # | Product Name | Grade and Purity | Mechanism and Research Application |
Recombinant KAT2A/GCN5 Antibody | Recombinant, ExactAb™, validated, see COA | Specifically detects KAT2A/GCN5; used to analyze relationships between acetyltransferase abundance and acetyl-CoA-dependent protein acetylation | |
Recombinant KAT2B/PCAF Antibody | Recombinant, ExactAb™, KD Validation, validated, see COA | Specifically detects KAT2B/PCAF; used to verify genetic interventions and analyze how changes in acetyltransferase abundance affect protein acetylation | |
Recombinant KAT8/MYST1/MOF Antibody | Recombinant, ExactAb™, validated, 2.0 mg/mL | Specifically detects KAT8/MOF; used to investigate its relationships with histone acetylation, chromatin state, and transcriptional regulation | |
Human K-acetyltransferase 5 (KAT5) ELISA Kit | BioReagent | Quantifies KAT5 protein by ELISA; used to compare acetyltransferase-regulatory levels under different metabolic or intervention conditions | |
Recombinant Human SIRT5 Protein | ≥90%(SDS-PAGE) | Possesses strong desuccinylase, demalonylase, and related deacylase activities; used in in vitro enzymatic assays, substrate-recognition studies, and acylation-regulation research | |
SIRT5 Mouse mAb | See COA | Specifically detects SIRT5 protein; used to analyze relationships among SIRT5 abundance, protein succinylation and malonylation, and mitochondrial metabolism | |
SIRT5 Human Pre-designed siRNA Set A | — | Downregulates SIRT5 through RNA interference; used to determine how SIRT5 loss affects protein succinylation, malonylation, and mitochondrial metabolic phenotypes | |
Human Sirtuin 5 (SIRT5) ELISA Kit | BioReagent | Quantifies SIRT5 protein by ELISA; used to analyze the relationship between SIRT5 abundance and mitochondrial protein-acylation states |
6.4 Products for CoA Biosynthesis and Organic Acid Metabolism
Catalog # | Product Name | Grade and Purity | Mechanism and Research Application |
3′-Dephosphocoenzyme A | ≥90% | CoA-biosynthesis-related intermediate; used to investigate the final steps of de novo CoA biosynthesis, COASY-associated reactions, and CoA generation. | |
COASY Human Pre-designed siRNA Set A | — | Downregulates COASY through RNA interference; used to verify the final steps of CoA biosynthesis and metabolic phenotypes associated with COASY deficiency. | |
Recombinant COASY Antibody | Recombinant, ExactAb™, KD Validation, validated, see COA | Specifically detects COASY protein; used to measure COASY expression, verify genetic interventions, and analyze relationships between COASY status and CoA availability. | |
Recombinant Methylmalonyl-CoA mutase Antibody | KD Validation | Detects methylmalonyl-CoA mutase; used to analyze methylmalonyl-CoA-to-succinyl-CoA conversion and related organic acid metabolism. |
Major Abbreviations
Abbreviation | Full Name | Definition |
CoA | Coenzyme A | Intracellular carrier of activated acyl groups |
Acyl-CoA | Acyl Coenzyme A | CoA derivative carrying an acyl group |
Acetyl-CoA | Acetyl Coenzyme A | Central two-carbon metabolite and acetyl-group donor |
Malonyl-CoA | Malonyl Coenzyme A | Fatty acid synthesis substrate and CPT1 regulator |
Succinyl-CoA | Succinyl Coenzyme A | TCA-cycle intermediate and succinyl-group donor |
Propionyl-CoA | Propionyl Coenzyme A | Intermediate in odd-chain fatty acid, amino acid, and propionate metabolism |
PANK | Pantothenate Kinase | Enzyme catalyzing the initial step of CoA biosynthesis |
COASY | CoA Synthase | Enzyme catalyzing the final steps of CoA biosynthesis |
ACLY | ATP Citrate Lyase | Enzyme producing cytosolic acetyl-CoA from citrate |
ACSS2 | Acetyl-CoA Synthetase 2 | Enzyme producing acetyl-CoA from acetate |
ACC | Acetyl-CoA Carboxylase | Enzyme generating malonyl-CoA from acetyl-CoA |
MCD | Malonyl-CoA Decarboxylase | Enzyme degrading malonyl-CoA |
CPT1 | Carnitine Palmitoyltransferase 1 | Regulatory enzyme controlling mitochondrial entry of long-chain fatty acyl groups |
PCC | Propionyl-CoA Carboxylase | Enzyme converting propionyl-CoA into methylmalonyl-CoA |
TCA | Tricarboxylic Acid Cycle | Central mitochondrial oxidative metabolic cycle |
HDAC | Histone Deacetylase | Enzyme removing acetyl groups from histones and other proteins |
PKAN | Pantothenate Kinase-associated Neurodegeneration | Neurodegenerative disease associated with PANK2 dysfunction |
CoPAN | COASY Protein-associated Neurodegeneration | Neurodegenerative disease associated with COASY dysfunction |
MASLD | Metabolic Dysfunction-associated Steatotic Liver Disease | Metabolic liver disease characterized by excessive hepatic lipid accumulation |
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