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Information on EC 6.3.2.25 - tubulin-tyrosine ligase and Organism(s) Homo sapiens and UniProt Accession Q8NG68

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IUBMB Comments
L-Tyrosine is linked via a peptide bond to the C-terminus of de-tyrosinated alpha-tubulin (des-Tyromega-alpha-tubulin). The enzyme is highly specific for alpha-tubulin and moderately specific for ATP and L-tyrosine. L-Phenylalanine and 3,4-dihydroxy-L-phenylalanine are transferred but with higher Km values.
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This record set is specific for:
Homo sapiens
UNIPROT: Q8NG68
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ttl, tubulin tyrosine ligase, tubulin-tyrosine ligase, tubulin:tyrosine ligase, tubulin-tyrosine-ligase, tyrosyltubulin ligase, ttlase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Synthetase, tubulin-tyrosine
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-
-
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TTLase
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-
-
-
tubulin tyrosine ligase
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-
Tubulin:tyrosine ligase
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-
-
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Tyrosyltubulin ligase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formation of peptide bond
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-tubulin:L-tyrosine ligase (ADP-forming)
L-Tyrosine is linked via a peptide bond to the C-terminus of de-tyrosinated alpha-tubulin (des-Tyromega-alpha-tubulin). The enzyme is highly specific for alpha-tubulin and moderately specific for ATP and L-tyrosine. L-Phenylalanine and 3,4-dihydroxy-L-phenylalanine are transferred but with higher Km values.
CAS REGISTRY NUMBER
COMMENTARY hide
60321-03-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + detyrosinated alpha-tubulin + L-Tyr
alpha-tubulin + ADP + phosphate
show the reaction diagram
the enzyme plays a vital role in neuronal organization
-
-
?
ATP + detyrosinated alpha-tubulin + L-tyrosine
alpha-tubulin + ADP + phosphate
show the reaction diagram
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-
-
?
additional information
?
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-
the testis-specific apoptosis related gene TTL.6 (member of the tubulin-tyrosine ligase family) undergoes adaptive evolution in the lineage leading to humans
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + detyrosinated alpha-tubulin + L-Tyr
alpha-tubulin + ADP + phosphate
show the reaction diagram
the enzyme plays a vital role in neuronal organization
-
-
?
ATP + detyrosinated alpha-tubulin + L-tyrosine
alpha-tubulin + ADP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
the testis-specific apoptosis related gene TTL.6 (member of the tubulin-tyrosine ligase family) undergoes adaptive evolution in the lineage leading to humans
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
required for the N-formyl-Met-Leu-Phe-induced and the antibiotic A23187-induced stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,4aS,6R,8S)-6,8-dihydroxy-5-[(3E)-5-hydroxy-5-(3-hydroxy-5-oxo-2,5-dihydrofuran-2-yl)-3-methylpent-3-en-1-yl]-4a,6-dimethyldecahydronaphthalene-1-carboxylic acid
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increases the non-tyrosinatable form of alpha-tubulin in human cancer cell cultures indicating to act as an inhibitor of TTL
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
A23187
-
Ca2+ is required for the N-formyl-Met-Leu-Phe-induced and the A23187-induced stimulation
N-Formyl-Met-Leu-Phe
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Ca2+ is required for the N-formyl-Met-Leu-Phe-induced and the A23187-induced stimulation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
preferentially expressed in adult and fetal brain
Manually annotated by BRENDA team
preferentially expressed in adult and fetal lung
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TTL_HUMAN
377
0
43212
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
loaded with binding partners, mass spectrometry
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK293T cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nath, J.; Gallin, J.I.
Ionic requirement and subcellular localization of tubulin tyrosinolation in human polymorphonuclear leucocytes
J. Immunol.
136
628-635
1986
Homo sapiens
Manually annotated by BRENDA team
Lafanechere, L.; Courtay-Cahen, C.; Kawakami, T.; Jacrot, M.; Rudiger, M.; Wehland, J.; Job, D.; Margolis, R.L.
Suppression of tubulin tyrosine ligase during tumor growth
J. Cell Sci.
111
171-181
1998
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Erck, C.; Peris, L.; Andrieux, A.; Meissirel, C.; Gruber, A.D.; Vernet, M.; Schweitzer, A.; Saoudi, Y.; Pointu, H.; Bosc, C.; Salin, P.A.; Job, D.; Wehland, J.
A vital role of tubulin-tyrosine-ligase for neuronal organization
Proc. Natl. Acad. Sci. USA
102
7853-7858
2005
Mus musculus, Homo sapiens (Q8NG68)
Manually annotated by BRENDA team
Chen, X.H.; Shi, H.; Liu, X.L.; Su, B.
The testis-specific apoptosis related gene TTL.6 underwent adaptive evolution in the lineage leading to humans
Gene
370
58-63
2006
Homo sapiens
Manually annotated by BRENDA team
Dal Piaz, F.; Vassallo, A.; Lepore, L.; Tosco, A.; Bader, A.; De Tommasi, N.
Sesterterpenes as tubulin tyrosine ligase inhibitors. First insight of structure-activity relationships and discovery of new lead
J. Med. Chem.
52
3814-3828
2009
Homo sapiens
Manually annotated by BRENDA team