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Information on EC 3.4.13.23 - cysteinylglycine-S-conjugate dipeptidase and Organism(s) Corynebacterium striatum and UniProt Accession B2KZE7

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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This record set is specific for:
Corynebacterium striatum
UNIPROT: B2KZE7
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The taxonomic range for the selected organisms is: Corynebacterium striatum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
cytosolic aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiol precursor dipeptidase
-
lap3
-
-
-
-
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
L-Glu-L-Trp + H2O
L-glutamate + L-tryptophan
show the reaction diagram
-
-
-
?
L-Ile-L-Asn + H2O
L-isoleucine + L-asparagine
show the reaction diagram
-
-
-
?
L-Leu-L-Ala + H2O
L-leucine + L-alanine
show the reaction diagram
-
-
-
?
L-Leu-L-Asn + H2O
L-leucine + L-asparagine
show the reaction diagram
-
-
-
?
L-Trp-L-Leu + H2O
L-tryptophan + L-leucine
show the reaction diagram
-
-
-
?
L-Val-L-Lys + H2O
L-valine + L-lysine
show the reaction diagram
-
-
-
?
S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine + H2O
S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteine + glycine
show the reaction diagram
-
-
-
?
S-benzyl-L-Cys-Gly + H2O
S-benzyl-L-Cys + glycine
show the reaction diagram
-
-
-
?
additional information
?
-
enzyme hydrolyzes a relatively broad range of dipeptides such as Trp-Leu, Glu-Trp, Ile-Asn, Leu-Ala, but it is not able to cleave acidic amino acids from the C terminus or to cleave Cys-Gly
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
pyridine-2,6-dicarboxylic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine
pH 7.0, temperature not specified in the publication
0.2
S-benzyl-L-Cys-Gly
pH 7.0, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
1,10-phenanthroline
Corynebacterium striatum
pH 7.0, temperature not specified in the publication
0.015
pyridine-2,6-dicarboxylic acid
Corynebacterium striatum
pH 7.0, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is involved in formation of human axillary odor by the action of Corynebacteria on odorless axilla secretions. Co-incubation of either a synthetic Cys-Gly-S conjugate or fresh axilla secretions with both the C-S lyase and the dipeptidase TpdA releases the odorant 3-methyl-3-sulfanylhexan-1-ol
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPDA_CORST
455
0
49000
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Emter, R.; Natsch, A.
The sequential action of a dipeptidase and a beta-lyase is required for the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a secreted Cys-Gly-S conjugate by Corynebacteria
J. Biol. Chem.
283
20645-20652
2008
Corynebacterium striatum (B2KZE7)
Manually annotated by BRENDA team