Aspartate Aminotransferase: Difference between revisions
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==Function== | ==Function== | ||
'''Aspartate Aminotransferase''' (AAT), also known as '''Glutamic aspartic transaminase''', '''glutamic oxaloacetic transaminase''', '''prephenate aminotransferase''' and '''transaminase A''' is an enzyme that is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family <ref name ="AST family and name">PMID:20977429</ref>. It is coded by the gene GOT1<ref name ="AST gene">PMID:4193185</ref>. It is a homodimer that is 413 amino acids long and serves a critical role in amino acid and carbohydrate metabolism, ureogenesis, and the transfer of reducing equivalents into the mitochondria and chloroplast<ref name ="AST ROLES AND STRUCTURE">PMID:10708649</ref>. Within prokaryote cells it is exclusively found in the cytosol, but in eukaryotic cells there are cytosol, mitochondrial, and chloroplast isozymes<ref name ="AST family and name"/><ref name ="AST Structure"/>. '''Bifunctional aspartate aminotransferase''' (BAAT) is | '''Aspartate Aminotransferase''' (AAT), also known as '''Glutamic aspartic transaminase''', '''glutamic oxaloacetic transaminase''', '''prephenate aminotransferase''' and '''transaminase A''' is an enzyme that is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family <ref name ="AST family and name">PMID:20977429</ref>. It is coded by the gene GOT1<ref name ="AST gene">PMID:4193185</ref>. It is a homodimer that is 413 amino acids long and serves a critical role in amino acid and carbohydrate metabolism, ureogenesis, and the transfer of reducing equivalents into the mitochondria and chloroplast<ref name ="AST ROLES AND STRUCTURE">PMID:10708649</ref>. Within prokaryote cells it is exclusively found in the cytosol, but in eukaryotic cells there are cytosol, mitochondrial, and chloroplast isozymes<ref name ="AST family and name"/><ref name ="AST Structure"/>. | ||
*'''Bifunctional aspartate aminotransferase''' (BAAT) is found in plants. It displays aspartate and prephanate aminotransferase activity<ref >PMID:24902885</ref>. | |||
In the human body it is produced in the brain, skeletal muscles, liver, pancreas, red blood cells, and kidneys <ref name ="AST ORGANS">PMID:2569674</ref><ref name ="Liver damage"/>. The wide range of tissues in which it is made, separates it from the similar enzyme alanine transaminase (ALT) which is found primarily in the liver<ref name ="Liver damage">PMID:10831269</ref>. The level of AAT in the body can be used as a marker for tissue disease or damage<ref name ="Liver damage"/>. As well, AAT and ALT levels can be compared to pinpoint whether tissue damage is primarily found within the liver<ref name ="Liver damage">PMID:12546613</ref>. | In the human body it is produced in the brain, skeletal muscles, liver, pancreas, red blood cells, and kidneys <ref name ="AST ORGANS">PMID:2569674</ref><ref name ="Liver damage"/>. The wide range of tissues in which it is made, separates it from the similar enzyme alanine transaminase (ALT) which is found primarily in the liver<ref name ="Liver damage">PMID:10831269</ref>. The level of AAT in the body can be used as a marker for tissue disease or damage<ref name ="Liver damage"/>. As well, AAT and ALT levels can be compared to pinpoint whether tissue damage is primarily found within the liver<ref name ="Liver damage">PMID:12546613</ref>. | ||