| Protein | Synonyms | Taxonomy |
|---|
| 3-hydroxypropionyl-coenzyme A synthetase | 3-hydroxypropionyl-CoA synthetase; EC 6.2.1.36 | Metallosphaera sedula DSM 5348 |
| Malonyl CoA reductase (NADP) | EC 1.2.1.75; NADP-dependent malonyl CoA reductase | Metallosphaera sedula DSM 5348 |
| Malonyl-CoA reductase | EC 1.2.1.75 | Sulfurisphaera tokodaii str. 7 |
| Biotin carboxyl carrier protein | | Metallosphaera sedula DSM 5348 |
| Aldehyde Dehydrogenase | | Pyrobaculum neutrophilum V24Sta |
| Acryloyl-coenzyme A reductase | Acryloyl-CoA reductase; EC 1.3.1.84 | Sulfurisphaera tokodaii str. 7 |
| 3-hydroxypropionyl-coenzyme A dehydratase | 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 | Metallosphaera sedula DSM 5348 |
| Succinate-semialdehyde dehydrogenase (acetylating) | EC 1.2.1.76 | Metallosphaera sedula DSM 5348 |
| 4-hydroxybutyrate--CoA ligase 1 | EC 6.2.1.40; Acetate--CoA ligase; 6.2.1.1; Butyrate--CoA ligase; 6.2.1.2; Propionate--CoA ligase; 6.2.1.17 | Metallosphaera sedula DSM 5348 |
| Vinylacetyl-CoA Delta-isomerase | | Metallosphaera sedula DSM 5348 |
| Acetyl-CoA carboxylase carboxyltransferase subunit alpha / acetyl-CoA carboxylase carboxyltransferase subunit beta / propionyl-CoA carboxylase carboxyltransferase subunit | | Metallosphaera sedula DSM 5348 |
| Biotin carboxylase | | Metallosphaera sedula DSM 5348 |
| Enoyl-CoA hydratase | | Metallosphaera sedula DSM 5348 |
| Methylmalonyl-CoA mutase | | Metallosphaera sedula DSM 5348 |
| Methylmalonyl-CoA epimerase | | Metallosphaera sedula DSM 5348 |
| Acetyl-CoA acetyltransferase | | Metallosphaera sedula DSM 5348 |
| 3-hydroxypropionate dehydrogenase | | Metallosphaera sedula DSM 5348 |
| Cobalamin B12-binding domain protein | | Metallosphaera sedula DSM 5348 |
| Compound | Description |
|---|
| diphosphoric acid | |
| hydronium ion | |
| Cobalt | A trace element that is a component of vitamin B12. It has the atomic symbol Co, atomic number 27, and atomic weight 58.93. It is used in nuclear weapons, alloys, and pigments. Deficiency in animals leads to anemia; its excess in humans can lead to erythrocytosis. |
| NADH | |
| Carbon Dioxide | A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals. |
| 4-hydroxybutyric acid | was an entry term to Sodium Oxybate (74-98) |
| 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 | |
| adenosine diphosphate | Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. |
| hydrogen carbonate | |
| 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. |
| Nickel | A trace element with the atomic symbol Ni, atomic number 28, and atomic weight 58.69. It is a cofactor of the enzyme UREASE. |
| 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 | |
| iodoacetamide | An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate. |
| cobamamide | |
| 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) |
| 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 | |
| dithioerythritol | A compound that, along with its isomer, Cleland's reagent (DITHIOTHREITOL), is used for the protection of sulfhydryl groups against oxidation to disulfides and for the reduction of disulfides to sulfhydryl groups. |
| acetoacetyl CoA | |
| 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. |
| Dihydroergocristine | A 9,10alpha-dihydro derivative of ERGOTAMINE that contains an isopropyl sidechain at the 2' position of the molecule. |
| Malonyl Coenzyme A | A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems. |
| propionyl-coenzyme A | RN given refers to parent cpd |
| 4-hydroxybutyryl-coenzyme A | structure given in first source |
| 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) |