Sandbox Reserved 346: Difference between revisions
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{{Template:Sandbox_Reserved_BCMB307}} | {{Template:Sandbox_Reserved_BCMB307}} | ||
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=='''Function'''== | =='''Function'''== | ||
AST catalyzes the reversible transamination of the alpha-amino group from L-aspartate alpha-ketoglutarate. This reactivity is lower in ''E.coli'' than in higher eukaryotes, and had borader substrate specificity. However, the reaction takes place in the same way. Upon introduction of an amino acid substrate, a new Schiff base will form between it and the PLP cofactor. This causes the amino acid to lose a hydrogen to form the quinoid intermediate, and reprotanation takes place resulting in a ketimine. Next, the structure is hydrolyzed forming an alpha-keto acid and pyridoxamine phosphate. 2-methyl asparate acts as an inhibitor of AST when it forms a Schiif base with the PLP cofactor, rather than aspartate. This results in the process stopping at the step prior to the alpha protein elimination. | |||
=='''Clinical Applications'''== | =='''Clinical Applications'''== | ||
=='''Additional Resources'''== | =='''Additional Resources'''== | ||
=='''References'''== | =='''References'''== | ||