Information on EC 6.3.2.B3 - tubulin-glutamate ligase

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The expected taxonomic range for this enzyme is: Tetrahymena thermophila

EC NUMBER
COMMENTARY hide
6.3.2.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
tubulin-glutamate ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + alpha-tubulin + L-glutamate = L-glutamyl-alpha-tubulin + ADP + phosphate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
alpha-tubulin:L-glutamate ligase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
show the reaction diagram
additional information
?
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Ttll1p and Ttll9p are tubulin tyrosine ligase domain proteins, that act as alpha-tubulin-preferring glutamyl ligase enzymes, TTLL1- and TLLL9-type enzymes are highly conserved but are absent from higher plants and fungi, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
show the reaction diagram
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glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles, the spatial restriction of modifying enzymes appears to be a major mechanism that drives differential glutamylation at the subcellular level
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?
additional information
?
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Ttll1p and Ttll9p are tubulin tyrosine ligase domain proteins, that act as alpha-tubulin-preferring glutamyl ligase enzymes, TTLL1- and TLLL9-type enzymes are highly conserved but are absent from higher plants and fungi, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial purification of recombinant GFP-tagged Ttll1p and GFP-tagged Ttll9p
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of GFP-tagged Ttll1p mainly in the basal bodies and of GFP-tagged Ttll9p mainly in the cilia of CU428 and B2086 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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disruption of the TTLL1 and TTLL9 genes decrease the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies, in the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs, phenotype, overview