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Detyrosination
From Wikipedia, the free encyclopedia
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Detyrosination is a form of posttranslational modification that occurs on alpha-tubulin.[1] It consists of the removal of the C-terminal tyrosine to expose a glutamate at the newly formed C-terminus. Tubulin polymers, called microtubules, that contain detyrosinated alpha-tubulin are usually referred to as Glu-microtubules while unmodified polymers are called Tyr-microtubules.
The detyrosynating activity was first identified in the late 1970s.[2] It is a slow acting enzyme that uses polymeric tubulin as a substrate. As a result, only stabilized microtubules accumulate this particular modification. Tubulin detyrosination is reversed by the tubulin-tyrosine ligase,[3] which acts only on alpha-tubulin monomer. Since the majority of microtubules are very dynamic, they do not contain much detyrosinated tubulin.
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