Enzymes
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Name help_outline
(L-glutamyl)n-γ-L-glutamyl-L-glutamate residue
Identifier
CHEBI:143623
Charge
-3
Formula
(C5H6NO3)n.C10H12N2O6
Search links
Involved in 4 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:15519Polymer name: (L-glutamyl)(n)-γ-L-glutamyl-L-glutamyl-[protein]Polymerization index help_outline nFormula C10H12N2O6(C5H6NO3)nCharge (-2)(-1)nMol File for the polymer
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Identifier: RHEA-COMP:15675Polymer name: (L-glutamyl)(n+1)-γ-L-glutamyl-L-glutamyl-[protein]Polymerization index help_outline n+1Formula C10H12N2O6(C5H6NO3)n+1Charge (-2)(-1)n+1Mol File for the polymer
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- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 244 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,284 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,002 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:60148 | RHEA:60149 | RHEA:60150 | RHEA:60151 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Gene Ontology help_outline |
Related reactions help_outline
Specific form(s) of this reaction
Publications
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Writing and Reading the Tubulin Code.
Yu I., Garnham C.P., Roll-Mecak A.
Microtubules give rise to intracellular structures with diverse morphologies and dynamics that are crucial for cell division, motility, and differentiation. They are decorated with abundant and chemically diverse posttranslational modifications that modulate their stability and interactions with c ... >> More
Microtubules give rise to intracellular structures with diverse morphologies and dynamics that are crucial for cell division, motility, and differentiation. They are decorated with abundant and chemically diverse posttranslational modifications that modulate their stability and interactions with cellular regulators. These modifications are important for the biogenesis and maintenance of complex microtubule arrays such as those found in spindles, cilia, neuronal processes, and platelets. Here we discuss the nature and subcellular distribution of these posttranslational marks whose patterns have been proposed to constitute a tubulin code that is interpreted by cellular effectors. We review the enzymes responsible for writing the tubulin code, explore their functional consequences, and identify outstanding challenges in deciphering the tubulin code. << Less
J Biol Chem 290:17163-17172(2015) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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Tubulin polyglutamylase enzymes are members of the TTL domain protein family.
Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B.
Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase-like (TTLL) protein, TTLL1. ... >> More
Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase-like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila, two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization. << Less
Science 308:1758-1762(2005) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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A targeted multienzyme mechanism for selective microtubule polyglutamylation.
van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.
Polyglutamylases are enzymes that form polyglutamate side chains of variable lengths on proteins. Polyglutamylation of tubulin is believed to regulate interactions of microtubules (MTs) with MT-associated proteins and molecular motors. Subpopulations of MTs are differentially polyglutamylated, yet ... >> More
Polyglutamylases are enzymes that form polyglutamate side chains of variable lengths on proteins. Polyglutamylation of tubulin is believed to regulate interactions of microtubules (MTs) with MT-associated proteins and molecular motors. Subpopulations of MTs are differentially polyglutamylated, yet only one modifying enzyme has been discovered in mammals. In an attempt to better understand the heterogeneous appearance of tubulin polyglutamylation, we searched for additional enzymes and report here the identification of six mammalian polyglutamylases. Each of them has a characteristic mode of catalysis and generates distinct patterns of modification on MTs, which can be further diversified by cooperation of multiple enzymes. Polyglutamylases are restricted to confined tissues and subtypes of MTs by differential expression and localization. In conclusion, we propose a multienzyme mechanism of polyglutamylation that can explain how the diversity of polyglutamylation on selected types of MTs is controlled at the molecular level. << Less
Mol. Cell 26:437-448(2007) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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Structure of the polyglutamyl side chain posttranslationally added to alpha-tubulin.
Redeker V., Le Caer J.P., Rossier J., Prome J.C.
Polyglutamylation, a new posttranslational modification of tubulin identified originally on the acidic alpha variants by Eddé et al. (Eddé, B., Rossier, J., Le Caer, J. P., Desbruyeres, E., Gros, F., and Denoulet, P. (1990) Science 247, 83-85), consists of the successive addition of glutamyl units ... >> More
Polyglutamylation, a new posttranslational modification of tubulin identified originally on the acidic alpha variants by Eddé et al. (Eddé, B., Rossier, J., Le Caer, J. P., Desbruyeres, E., Gros, F., and Denoulet, P. (1990) Science 247, 83-85), consists of the successive addition of glutamyl units to the Glu445. To characterize their linkage mode mouse tubulin was posttranslationally labeled with [3H]glutamate. After digestion of [3H]tubulin with thermolysin, up to eight radioactive peaks were separated on an anion exchange column (DEAE). Combined use of Edman degradation sequencing and mass spectrometry analysis of the first 6 one indicated that they all correspond to the same COOH-terminal sequence 440VEGEGEEEGEE450 bearing one to six glutamyl units on the Glu445. The first glutamyl residue is amide-linked to the gamma-carboxyl group of Glu445, but the additional residues can be linked to the gamma- or alpha-carboxyl groups of the preceding one. All possible linkages for the biglutamylated tubulin peptides (gamma 1 alpha 2, gamma 1 gamma 2) and triglutamylated (gamma 1 alpha 2 alpha 3, gamma 1 alpha 2 gamma 3, gamma 1 alpha 2 gamma 2, gamma 1 gamma 2 alpha 3, gamma 1 gamma 2 gamma 3) were synthesized. These different peptides were successfully separated on a C18 5-micron reverse phase column. We found that the bi- and triglutamylated tubulin peptides behave as the gamma 1 alpha 2 and gamma 1 alpha 2 alpha 3 synthetic peptides, respectively. These results indicate that the second and third glutamyl residues of the polyglutamyl side chain are amide-linked to the alpha-carboxyl group of the preceding unit. << Less
J Biol Chem 266:23461-23466(1991) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
Comments
For elongation, n is normally in the range of 3-8. For tubulin, the highest number known is n=21.