Literature summary for 2.3.1.108 extracted from

Maruta, H.; Greer, K.; Rosenbaum, J.L.
The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules (1986), J. Cell Biol., 103, 571-579.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Ca2+	at 1 mM, almost complete inhibition; inhibition is due to the binding of calcium to the tubulin dimer rather than to the enzyme itself	Chlamydomonas reinhardtii
CoA	competitive inhibitor	Chlamydomonas reinhardtii
Colchicine	at 0.001 mM is inhibitory to microtubule acetylation	Chlamydomonas reinhardtii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.002	-	acetyl-CoA	-	Chlamydomonas reinhardtii

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
flagellum	-	Chlamydomonas reinhardtii	-	-
microtubule	enzyme acetylated both dimers and polymers of tubulin	Chlamydomonas reinhardtii	5874	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
67000	-	2 * 67000, SDS-PAGE	Chlamydomonas reinhardtii
130000	-	gel filtration	Chlamydomonas reinhardtii

Organism

Organism	UniProt	Comment	Textmining
Chlamydomonas reinhardtii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Chlamydomonas reinhardtii

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + alpha-tubulin L-lysine	alpha-tubulin from Chlamydomonas is acetylated	Chlamydomonas reinhardtii	CoA + alpha-tubulin N6-acetyl-L-lysine	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 67000, SDS-PAGE	Chlamydomonas reinhardtii

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.008	-	CoA	competitive inhibitor	Chlamydomonas reinhardtii

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Release 2023.1 (January 2023)