Enzymes
| UniProtKB help_outline | 3 proteins |
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Namehelp_outline
C-terminal L-α-aminoacyl-L-glutamyl-L-glutamyl-L-phenylalanyl-[tubulin]
Identifier
RHEA-COMP:18133
Reactive part
help_outline
- Name help_outline C-terminal L-α-amino-acyl-L-glutamyl-L-glutamyl-L-phenylalanine residue Identifier CHEBI:192362 Charge -3 Formula C21H23N4O9R SMILEShelp_outline N([C@H](C(N[C@H](C(=O)N[C@H](C(=O)[O-])CC1=CC=CC=C1)CCC(=O)[O-])=O)CCC(=O)[O-])C(=O)[C@@H](N*)* 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
C-terminal L-α-aminoacyl-L-glutamyl-L-glutamyl-[tubulin]
Identifier
RHEA-COMP:16435
Reactive part
help_outline
- Name help_outline C-terminal α-amino-acyl-L-glutamyl-L-glutamate residue Identifier CHEBI:149555 Charge -3 Formula C12H14N3O8R SMILEShelp_outline N([C@H](C(N[C@H](C(=O)[O-])CCC(=O)[O-])=O)CCC(=O)[O-])C(=O)[C@@H](N*)* 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-phenylalanine Identifier CHEBI:58095 Charge 0 Formula C9H11NO2 InChIKeyhelp_outline COLNVLDHVKWLRT-QMMMGPOBSA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccccc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 78 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:72663 | RHEA:72664 | RHEA:72665 | RHEA:72666 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Posttranslational modification of microtubules by the MATCAP detyrosinase.
Landskron L., Bak J., Adamopoulos A., Kaplani K., Moraiti M., van den Hengel L.G., Song J.Y., Bleijerveld O.B., Nieuwenhuis J., Heidebrecht T., Henneman L., Moutin M.J., Barisic M., Taraviras S., Perrakis A., Brummelkamp T.R.
The detyrosination-tyrosination cycle involves the removal and religation of the C-terminal tyrosine of α-tubulin and is implicated in cognitive, cardiac, and mitotic defects. The vasohibin-small vasohibin-binding protein (SVBP) complex underlies much, but not all, detyrosination. We used haploid ... >> More
The detyrosination-tyrosination cycle involves the removal and religation of the C-terminal tyrosine of α-tubulin and is implicated in cognitive, cardiac, and mitotic defects. The vasohibin-small vasohibin-binding protein (SVBP) complex underlies much, but not all, detyrosination. We used haploid genetic screens to identify an unannotated protein, microtubule associated tyrosine carboxypeptidase (MATCAP), as a remaining detyrosinating enzyme. X-ray crystallography and cryo-electron microscopy structures established MATCAP's cleaving mechanism, substrate specificity, and microtubule recognition. Paradoxically, whereas abrogation of tyrosine religation is lethal in mice, codeletion of MATCAP and SVBP is not. Although viable, defective detyrosination caused microcephaly, associated with proliferative defects during neurogenesis, and abnormal behavior. Thus, MATCAP is a missing component of the detyrosination-tyrosination cycle, revealing the importance of this modification in brain formation. << Less