Other grades of this product :
| Aspartate aminotransferase Basic information |
| Aspartate aminotransferase Chemical Properties |
| Safety Statements | 22-24/25 | | WGK Germany | 3 | | TSCA | Yes |
| Aspartate aminotransferase Usage And Synthesis |
| Uses | Converts L-aspartate and alpha-ketoglutarate to oxaloacetate and L-glutamate | | Definition | An enzyme that catalyzes reversibly the transfer of an amino group from glutamic acid to oxaloacetic acid, yielding α-ketoglutaric acid and aspartic acid. The codons for aspartate are GAC and GAU. | | General Description | Glutamic-Oxalacetic Transaminase is found in all tissues and is predominant in the liver and skeletal muscle. It is a prototype of fold-type I pyridoxal 5′-phosphate (PLP)-enzymes. Glutamic-oxalacetic transaminase is a homodimer containing large and small domains in each subunit. | | Biochem/physiol Actions | Glutamic-oxalacetic transaminase or aspartate aminotransferase (AAT) catalyzes the interconversion of L-aspartate and α-ketoglutarate with oxalacetate and L-glutamate. This reversible transaminase reaction is dependent on pyridoxal 5′-phosphate (PLP). Glutamic-oxalacetic transaminase maintains the nitrogen currency for metabolism by generating L-glutamate. Elevated serum levels of glutamic-oxalacetic transaminase are indicated in myocardial infarction, liver diseases, and some renal diseases. |
| Aspartate aminotransferase Preparation Products And Raw materials |
|
日本语
한국어
Français
Deutsch
España
Türkiye