Protein | Synonyms | Taxonomy |
2-oxoglutarate dehydrogenase E1 component | EC 1.2.4.2; Alpha-ketoglutarate dehydrogenase | Escherichia coli K-12 |
Aconitate hydratase A | ACN; Aconitase; EC 4.2.1.3; Iron-responsive protein-like; IRP-like; RNA-binding protein; Stationary phase enzyme | Escherichia coli K-12 |
Aconitate hydratase B | ACN; Aconitase; EC 4.2.1.3; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; 2-methyl-cis-aconitate hydratase; 4.2.1.99; Iron-responsive protein-like; IRP-like; RNA-binding protein | Escherichia coli K-12 |
Malate:quinone oxidoreductase | EC 1.1.5.4; MQO; Malate dehydrogenase [quinone] | Escherichia coli K-12 |
Fumarate hydratase class II | Fumarase C; EC 4.2.1.2; Aerobic fumarase; Iron-independent fumarase | Escherichia coli K-12 |
Dihydrolipoyl dehydrogenase | EC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein | Escherichia coli K-12 |
Malate dehydrogenase | EC 1.1.1.37 | Escherichia coli K-12 |
Succinate--CoA ligase [ADP-forming] subunit beta | EC 6.2.1.5; Succinyl-CoA synthetase subunit beta; SCS-beta | Escherichia coli K-12 |
Succinate--CoA ligase [ADP-forming] subunit alpha | EC 6.2.1.5; Succinyl-CoA synthetase subunit alpha; SCS-alpha | Escherichia coli K-12 |
Citrate synthase | EC 2.3.3.16 | Escherichia coli K-12 |
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex | EC 2.3.1.61; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex | Escherichia coli K-12 |
Isocitrate dehydrogenase [NADP] | IDH; EC 1.1.1.42; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase | Escherichia coli K-12 |
Isocitrate dehydrogenase [NADP] | IDH; EC 1.1.1.42; Oxalosuccinate decarboxylase | Azotobacter vinelandii |
Fumarate hydratase class I, anaerobic | EC 4.2.1.2; D-tartrate dehydratase; 4.2.1.81; Fumarase B | Escherichia coli K-12 |
Fumarate hydratase class I, aerobic | EC 4.2.1.2; Fumarase A; Oxaloacetate keto--enol-isomerase; OAAKE isomerase; Oxaloacetate tautomerase; 5.3.2.2 | Escherichia coli K-12 |
Fumarase D | EC 4.2.1.2 | Escherichia coli K-12 |
Fumarase E | EC 4.2.1.2 | Escherichia coli K-12 |
Compound | Description |
hydronium ion | |
Silver | An element with the atomic symbol Ag, atomic number 47, and atomic weight 107.87. It is a soft metal that is used medically in surgical instruments, dental prostheses, and alloys. Long-continued use of silver salts can lead to a form of poisoning known as ARGYRIA. |
Thiamine Pyrophosphate | The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX. |
Succinate | |
NADH | |
Mercury | A silver metallic element that exists as a liquid at room temperature. It has the atomic symbol Hg (from hydrargyrum, liquid silver), atomic number 80, and atomic weight 200.59. Mercury is used in many industrial applications and its salts have been employed therapeutically as purgatives, antisyphilitics, disinfectants, and astringents. It can be absorbed through the skin and mucous membranes which leads to MERCURY POISONING. Because of its toxicity, the clinical use of mercury and mercurials is diminishing. |
Manganese | A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035) |
Carbon Dioxide | A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals. |
serum p-component | close relation to C reactive protein; may be ovosomucoid |
Zinc | A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn. |
Orthophosphate | |
Superoxides | Highly reactive compounds produced when oxygen is reduced by a single electron. In biological systems, they may be generated during the normal catalytic function of a number of enzymes and during the oxidation of hemoglobin to METHEMOGLOBIN. In living organisms, SUPEROXIDE DISMUTASE protects the cell from the deleterious effects of superoxides. |
fumarates | Compounds based on fumaric acid. |
adenosine diphosphate | Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. |
potassium | An element in the alkali group of metals with an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte that plays a significant role in the regulation of fluid volume and maintenance of the WATER-ELECTROLYTE BALANCE. |
Magnesium | A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION. |
Water | A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) |
succinyl-coenzyme A | |
phenylglyoxal | A reagent that is highly selective for the modification of arginyl residues. It is used to selectively inhibit various enzymes and acts as an energy transfer inhibitor in photophosphorylation. |
adenosine monophosphate | Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position. |
nad | A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) |
NADP | Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) |
NADP | Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) |
alpha-Ketoglutarate | |
Oxaloacetate | An anionic form of oxaloacetic acid. |
tungstate | |
Cadmium | An element with atomic symbol Cd, atomic number 48, and atomic weight 112.41. It is a metal and ingestion will lead to CADMIUM POISONING. |
glyoxylate | |
adenosine triphosphate | An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. |
Coenzyme A | |
Acetyl Coenzyme A | Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent. |
propionyl-coenzyme A | RN given refers to parent cpd |
Flavin-Adenine Dinucleotide | A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) |