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Information on EC 3.4.13.23 - cysteinylglycine-S-conjugate dipeptidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q01532

for references in articles please use BRENDA:EC3.4.13.23
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.13 Dipeptidases
                3.4.13.23 cysteinylglycine-S-conjugate dipeptidase
IUBMB Comments
The enzyme participates in a widespread glutathione-mediated detoxification pathway. In animals the activity is usually catalysed by enzymes that have numerous additional activities, such as EC 3.4.11.1, leucyl aminopeptidase, EC 3.4.11.2, membrane alanyl aminopeptidase, and EC 3.4.13.19, membrane dipeptidase. However, in the bacterium Corynebacterium sp. Ax20, which degrades axillary secretions, the enzyme appears to be specific for this task.
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Saccharomyces cerevisiae
UNIPROT: Q01532
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
cytosolic aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tpdA
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
cysteinylglycine-S-conjugate dipeptide hydrolase
The enzyme participates in a widespread glutathione-mediated detoxification pathway. In animals the activity is usually catalysed by enzymes that have numerous additional activities, such as EC 3.4.11.1, leucyl aminopeptidase, EC 3.4.11.2, membrane alanyl aminopeptidase, and EC 3.4.13.19, membrane dipeptidase. However, in the bacterium Corynebacterium sp. Ax20, which degrades axillary secretions, the enzyme appears to be specific for this task.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
enzyme displays broad specificity, cleaving substrate with beta-naphthylamine as chromophore and also the corresponding 4-nitroanilides. Enzyme hydrolyzes aminopeptidase substrates with a neutral or basic amino acid and L-Glu-beta-naphthylamide
-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
Lap3 is spatially associated with Ape1 and selectively transported to the vacuole during nitrogen starvation. Gene products ATG11 and ATG19 are important for Lap3 transport. Lap3 is degraded within a couple of hours in the vacuole
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
deletion of the BLHl gene is not lethal under normal growth conditions. blhl mutants show hypersensitivity to bleomycin
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 55400, calculated from sequence and SDS-PAGE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kageyama, T.; Suzuki, K.; Ohsumi, Y.
Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
378
551-557
2009
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Enenkel, C.; Wolf, D.H.
BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase
J. Biol. Chem.
268
7036-7043
1993
Saccharomyces cerevisiae (Q01532)
Manually annotated by BRENDA team