Information on EC 3.4.17.17 - tubulinyl-Tyr carboxypeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.17.17
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RECOMMENDED NAME
GeneOntology No.
tubulinyl-Tyr carboxypeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of the -Glu!Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
73050-23-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-tubulin + H2O
detyrosinated tubulin + Tyr
show the reaction diagram
tyrosinated tubulin + H2O
tubulin + Tyr
show the reaction diagram
additional information
?
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may have the ability to remove C-terminal Tyr residues from proteins based on both its substrate binding pocket and the loops surrounding the active site pocket. Has enzymatic activity toward small peptides that contain C-terminal hydrophobic groups
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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
alpha-tubulin + H2O
detyrosinated tubulin + Tyr
show the reaction diagram
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the enzyme could be part of the mechanism that regulates the tyrosination state of microtubules
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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activates, maximal activation at 4-6 mM
Zn2+
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zinc ligands
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(CH3)2SO
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2-mercaptoethanol
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benzyloxycarbonyl-Glu-Phe
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Benzyloxycarbonyl-Glu-Tyr
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Brain soluble RNA
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chondroitin sulfate
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cnicin
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heparin
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polylysine counteracts
ID3
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monoclonal antibody directed against the active site of TTL
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iodoacetate
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MgCl2
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myelin basic protein
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N-Carbobenzoxy dipeptides
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parthenolide
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efficiently inhibits. Inhibition of TCP activity is independent of NF-kappaB inhibition; inhibition of tubulin carboxypeptidase could be one of the mechanisms underlying the anticancer properties of parthenolide
phenylacetate
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Polyadenylic acid
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Polyglutamic acid
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proteoglycan
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putrescine
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inhibition above 6 mM
spermidine
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inhibition above 1 mM
spermine
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above 0.06 mM
ZnCl2
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
putrescine
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maximal stimulation at 6 mM
spermidine
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stimulates, maximal stimulation at 1 mM, inhibition above
spermine
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maximal stimulation at 0.06 mM
additional information
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MAP1B heavy chain may enhance TTL activity. Interaction between microtubule-associated protein 1B and TTL is not regulated by MAP1B phosphorylation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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N2a cells, high level of MAP1B expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
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gel filtration
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heparin protects against inactivation
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very unstable in purified preparation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AGBL4 expressed as a fusion protein with a thrombin-cleavable His-tag and a factor Xa-cleavable S-tag at the N-terminus in Escherichia coli BL21-Gold(DE3) cells
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expressed in COS-7 cells
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expression of TTL together with different MAP1B constructs (full-length MAP1B, MAP1B heavy chain and MAP1B light chain 1) in COS-7 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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MAP1B mutant, loss of MAP1B is deleterious for the efficient tyrosination of microtubules both in vitro and in vivo
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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TCP may be a target for developing novel therapeutic strategies against advanced stages of cancers. Inhibitors of TCP, by reversing abnormal detyrosinated tubulin accumulation in tumor cells, may impair tumor progression
additional information