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Information on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M0G0

for references in articles please use BRENDA:EC3.4.19.13
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.13 glutathione gamma-glutamate hydrolase
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Arabidopsis thaliana
UNIPROT: Q9M0G0 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hp1118, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
At4g29210
locus name
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione S-bimane + H2O
L-cysteinylglycyl S-bimane + L-glutamate
show the reaction diagram
-
-
-
?
glutathione-S-monobromobimane conjugate + H2O
L-cysteinylglycine-S-monobrombimane conjugate + L-glutamate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acivicin
in cells treated with the xenobiotic monochlorobimane, application of acivicin leads to accumulation of glutathione S-bimane conjugates
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform GGT3 is a major contributor to total enzymic activity in roots, but a relatively minor contributor in other tissues
Manually annotated by BRENDA team
additional information
isoform GGT3 is transcribed at relatively high levels in all parts of the plant. It is a major contributor to total enzymic activity in roots, but a relatively minor contributor in other tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GAGT3_ARATH
637
1
69148
Swiss-Prot
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grzam, A.; Martin, M.N.; Hell, R.; Meyer, A.J.
gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
FEBS Lett.
581
3131-3138
2007
Arabidopsis thaliana (Q9M0G0)
Manually annotated by BRENDA team
Ohkama-Ohtsu, N.; Oikawa, A.; Zhao, P.; Xiang, C.; Saito, K.; Oliver, D.J.
A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis
Plant Physiol.
148
1603-1613
2008
Arabidopsis thaliana (Q9M0G0)
Manually annotated by BRENDA team