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Literature summary for 2.3.2.2 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
Search for more literature for 2.3.2.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Allium cepa

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Allium cepa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Allium cepa

Purification (Commentary)

Purification (Comment) Organism
-
 Allium cepa

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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