TPDA_CORST
ID TPDA_CORST Reviewed; 455 AA.
AC B2KZE7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000305|PubMed:18515361};
DE EC=3.4.13.23 {ECO:0000269|PubMed:18515361};
DE AltName: Full=Thiol precursor dipeptidase {ECO:0000303|PubMed:18515361};
GN Name=tpdA {ECO:0000303|PubMed:18515361};
OS Corynebacterium striatum.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=43770;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Ax20;
RX PubMed=18515361; DOI=10.1074/jbc.m800730200;
RA Emter R., Natsch A.;
RT "The sequential action of a dipeptidase and a beta-lyase is required for
RT the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a
RT secreted Cys-Gly-(S) conjugate by Corynebacteria.";
RL J. Biol. Chem. 283:20645-20652(2008).
CC -!- FUNCTION: Metallopeptidase that hydrolyzes the Cys-Gly bond of Cys-Gly-
CC S-conjugates (PubMed:18515361). Involved in the formation of the human
CC body odorant 3-methyl-3-sulfanylhexan-1-ol (3M3SH) from odorless axilla
CC secretions. Catalyzes the hydrolysis of the Cys-Gly bond of the Cys-
CC Gly-S-conjugate of 3M3SH, a key precursor secreted by apocrine glands
CC in human axilla skin. The Cys-S-conjugate obtained is then cleaved by
CC the Cys-S-conjugate beta-lyase MetC, which finally releases 3M3SH
CC (PubMed:18515361). {ECO:0000269|PubMed:18515361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000269|PubMed:18515361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000303|PubMed:18515361};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine =
CC glycine + S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteine;
CC Xref=Rhea:RHEA:62572, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145804, ChEBI:CHEBI:145805;
CC Evidence={ECO:0000269|PubMed:18515361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62573;
CC Evidence={ECO:0000303|PubMed:18515361};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000269|PubMed:18515361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000303|PubMed:18515361};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P44514};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.045 mM for S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine
CC {ECO:0000269|PubMed:18515361};
CC KM=0.2 mM for S-benzyl-L-cysteinylglycine
CC {ECO:0000269|PubMed:18515361};
CC Vmax=0.023 mmol/min/mg enzyme with S-(1-hydroxy-3-methylhexan-3-yl)-
CC L-cysteinylglycine as substrate {ECO:0000269|PubMed:18515361};
CC Vmax=0.169 mmol/min/mg enzyme with S-benzyl-L-cysteinylglycine as
CC substrate {ECO:0000269|PubMed:18515361};
CC -!- SIMILARITY: Belongs to the peptidase M20F family. {ECO:0000305}.
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DR EMBL; EU311559; ACA03770.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KZE7; -.
DR SMR; B2KZE7; -.
DR KEGG; ag:ACA03770; -.
DR BioCyc; MetaCyc:MON-20503; -.
DR BRENDA; 3.4.13.23; 7918.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cobalt; Dipeptidase; Hydrolase; Metal-binding; Protease;
KW Zinc.
FT CHAIN 1..455
FT /note="Cysteinylglycine-S-conjugate dipeptidase"
FT /id="PRO_0000451211"
FT ACT_SITE 94
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P44514"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P44514"
SQ SEQUENCE 455 AA; 49000 MW; 9035C5B7483BC161 CRC64;
MSNDKAATST NFNLTPNRER IFQELSELIS HYSPHSMPEH ADTHEEAAKW VTAKLEELGL
DVTRHPTVDD ADTIIGVKEP VGDAPTILLY SHYDVVPAQN PAVWTNDPLE LDERDGRWYG
RGAADCKGNV IMHLEALRMV QENGGTDLGL KVVMEGSEEL GGEDGLGKLI DANPELFTAD
VIFIGDGGNV AVGIPTLTTH LRGGAQLRFK VDTLEGPVHS GGWGGAAPDA AHALIRIIDS
FFDEHGRTTI EGVDTTAKWE GDPYDRETFR KDARVLDGVQ LLGTVDDEPA DMVWARPAIT
VIGFTSVPVE DATNIVNPTA EAQFNLRVPA PQSAAEVAKK VEEQIRARAP WGAKVEVSIT
GVNEPFSTDP NGPAVQHFGK CLQDAYGAEH LTVVGTGGSI PLTVTLQKHF PDAEFALYGV
ADPAANIHGV DESVDPTEIE HVAIAEAEFL LTYGK
