| IED ID | IndEnz0002012173 |
| Enzyme Type ID | protease012173 |
| Protein Name |
Cysteinylglycine-S-conjugate dipeptidase EC 3.4.13.23 Thiol precursor dipeptidase |
| Gene Name | tpdA |
| Organism | Corynebacterium striatum |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Corynebacteriaceae Corynebacterium Corynebacterium striatum |
| Enzyme Sequence | MSNDKAATSTNFNLTPNRERIFQELSELISHYSPHSMPEHADTHEEAAKWVTAKLEELGLDVTRHPTVDDADTIIGVKEPVGDAPTILLYSHYDVVPAQNPAVWTNDPLELDERDGRWYGRGAADCKGNVIMHLEALRMVQENGGTDLGLKVVMEGSEELGGEDGLGKLIDANPELFTADVIFIGDGGNVAVGIPTLTTHLRGGAQLRFKVDTLEGPVHSGGWGGAAPDAAHALIRIIDSFFDEHGRTTIEGVDTTAKWEGDPYDRETFRKDARVLDGVQLLGTVDDEPADMVWARPAITVIGFTSVPVEDATNIVNPTAEAQFNLRVPAPQSAAEVAKKVEEQIRARAPWGAKVEVSITGVNEPFSTDPNGPAVQHFGKCLQDAYGAEHLTVVGTGGSIPLTVTLQKHFPDAEFALYGVADPAANIHGVDESVDPTEIEHVAIAEAEFLLTYGK |
| Enzyme Length | 455 |
| Uniprot Accession Number | B2KZE7 |
| Absorption | |
| Active Site | ACT_SITE 94; /evidence=ECO:0000250|UniProtKB:P44514; ACT_SITE 158; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P44514 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103; EC=3.4.13.23; Evidence={ECO:0000269|PubMed:18515361};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445; Evidence={ECO:0000303|PubMed:18515361}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine = glycine + S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteine; Xref=Rhea:RHEA:62572, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145804, ChEBI:CHEBI:145805; Evidence={ECO:0000269|PubMed:18515361};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62573; Evidence={ECO:0000303|PubMed:18515361}; CATALYTIC ACTIVITY: Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145802, ChEBI:CHEBI:145803; Evidence={ECO:0000269|PubMed:18515361};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569; Evidence={ECO:0000303|PubMed:18515361}; |
| DNA Binding | |
| EC Number | 3.4.13.23 |
| Enzyme Function | FUNCTION: Metallopeptidase that hydrolyzes the Cys-Gly bond of Cys-Gly-S-conjugates (PubMed:18515361). Involved in the formation of the human body odorant 3-methyl-3-sulfanylhexan-1-ol (3M3SH) from odorless axilla secretions. Catalyzes the hydrolysis of the Cys-Gly bond of the Cys-Gly-S-conjugate of 3M3SH, a key precursor secreted by apocrine glands in human axilla skin. The Cys-S-conjugate obtained is then cleaved by the Cys-S-conjugate beta-lyase MetC, which finally releases 3M3SH (PubMed:18515361). {ECO:0000269|PubMed:18515361}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Cobalt;Dipeptidase;Hydrolase;Metal-binding;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,000 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.045 mM for S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine {ECO:0000269|PubMed:18515361}; KM=0.2 mM for S-benzyl-L-cysteinylglycine {ECO:0000269|PubMed:18515361}; Vmax=0.023 mmol/min/mg enzyme with S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine as substrate {ECO:0000269|PubMed:18515361}; Vmax=0.169 mmol/min/mg enzyme with S-benzyl-L-cysteinylglycine as substrate {ECO:0000269|PubMed:18515361}; |
| Metal Binding | METAL 92; /note=Zinc 1; via amino nitrogen; /evidence=ECO:0000250|UniProtKB:P44514; METAL 125; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P44514; METAL 125; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P44514; METAL 159; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P44514; METAL 163; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P44514; METAL 428; /note=Zinc 2; via amino nitrogen; /evidence=ECO:0000250|UniProtKB:P44514 |
| Rhea ID | RHEA:60444; RHEA:60445; RHEA:62572; RHEA:62573; RHEA:62568; RHEA:62569 |
| Cross Reference Brenda | 3.4.13.23; |