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Literature summary for 3.4.17.17 extracted from

  • Rodriguez de la Vega, M.; Sevilla, R.G.; Hermoso, A.; Lorenzo, J.; Tanco, S.; Diez, A.; Fricker, L.D.; Bautista, J.M.; Aviles, F.X.
    Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily (2007), FASEB J., 21, 851-865.
    View publication on PubMed
Search for more literature for 3.4.17.17

Activating Compound

Activating Compound Comment Organism Structure
ADP
-
 Caenorhabditis elegans
ATP
-
 Caenorhabditis elegans

Application

Application Comment Organism
additional information link between tubulinyl-Tyr carboxypeptidase and Nna1-like proteins Caenorhabditis elegans

Cloned(Commentary)

Cloned (Comment) Organism
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 Caenorhabditis elegans

Inhibitors

Inhibitors Comment Organism Structure
additional information enzymatic activity is salt-inactivated Caenorhabditis elegans
Z-Glu-Tyr
-
 Caenorhabditis elegans

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Caenorhabditis elegans 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc ligands Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Caenorhabditis elegans ?
-
 ?

Synonyms

Synonyms Comment Organism
AGBL4
-
 Caenorhabditis elegans
nervous system nuclear protein induced by axotomy
-
 Caenorhabditis elegans
Nna1-like peptidase
-
 Caenorhabditis elegans