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Literature summary extracted from

  • Shaw, M.; Pither-Joyce, M.; McManus, M.; McCallum, J.
    Purification, characterization and cloning of onion gamma-glutamyl transpeptidase (2005), Acta Hortic., 688, 139-141.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2
-
 Allium cepa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.2 membrane associated Allium cepa 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.2 additional information Allium cepa the enzyme is unlikely to function as a gamma-glutamyl hydrolase in vivo. It is possible that it could catalyze transpeptidation of precursors such as S-methyl glutathione during S-alkyl cysteine sulfoxide biosynthesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Allium cepa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.2.2 glycoprotein
-
 Allium cepa

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2
-
 Allium cepa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.2 bulb sprouting Allium cepa
-
2.3.2.2 leaf
-
 Allium cepa
-
2.3.2.2 root
-
 Allium cepa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 additional information the enzyme is unlikely to function as a gamma-glutamyl hydrolase in vivo. It is possible that it could catalyze transpeptidation of precursors such as S-methyl glutathione during S-alkyl cysteine sulfoxide biosynthesis Allium cepa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 heterodimer probably has heterodimer structure with the larger subunit of 38900 Da Allium cepa