Literature summary for 6.3.2.25 extracted from

Chang, S.; Flavin, M.
Tubulin tyrosination in Crithidia: modifying enzymes and modification states of tubulin (1988), Cell Motil. Cytoskeleton, 10, 400-409.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + detyrosinated alpha-tubulin + L-Tyr	Crithidia fasciculata	terminal Tyr is present in about 5% of flagellar alpha-chain from cells in stationary phase and 20% from cells from midlog phase. None is detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which higher state of tyrosinylation characterizes recently assembled or unstable microtubules, terminal Tyr is present only in the most stable polymer, the flagellar double microtubules	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Crithidia fasciculata	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + detyrosinated alpha-tubulin + L-Tyr	tyrosinates Crithidia tubulin but not brain tubulin and is specific for the alpha chain	Crithidia fasciculata	alpha-tubulin + ADP + phosphate	-	?
ATP + detyrosinated alpha-tubulin + L-Tyr	terminal Tyr is present in about 5% of flagellar alpha-chain from cells in stationary phase and 20% from cells from midlog phase. None is detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which higher state of tyrosinylation characterizes recently assembled or unstable microtubules, terminal Tyr is present only in the most stable polymer, the flagellar double microtubules	Crithidia fasciculata	?	-	?

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Release 2023.1 (January 2023)