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Literature summary extracted from

  • 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 (2008), J. Biol. Chem., 283, 20645-20652 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.13.23 expression in Escherichia coli Corynebacterium striatum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.13.23 1,10-phenanthroline
-
Corynebacterium striatum
3.4.13.23 pyridine-2,6-dicarboxylic acid
-
Corynebacterium striatum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.13.23 0.045
-
S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine pH 7.0, temperature not specified in the publication Corynebacterium striatum
3.4.13.23 0.2
-
S-benzyl-L-Cys-Gly pH 7.0, temperature not specified in the publication Corynebacterium striatum

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.23 Corynebacterium striatum B2KZE7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.13.23 L-Glu-L-Trp + H2O
-
Corynebacterium striatum L-glutamate + L-tryptophan
-
?
3.4.13.23 L-Ile-L-Asn + H2O
-
Corynebacterium striatum L-isoleucine + L-asparagine
-
?
3.4.13.23 L-Leu-L-Ala + H2O
-
Corynebacterium striatum L-leucine + L-alanine
-
?
3.4.13.23 L-Leu-L-Asn + H2O
-
Corynebacterium striatum L-leucine + L-asparagine
-
?
3.4.13.23 L-Trp-L-Leu + H2O
-
Corynebacterium striatum L-tryptophan + L-leucine
-
?
3.4.13.23 L-Val-L-Lys + H2O
-
Corynebacterium striatum L-valine + L-lysine
-
?
3.4.13.23 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 Corynebacterium striatum ?
-
?
3.4.13.23 S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine + H2O
-
Corynebacterium striatum S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteine + glycine
-
?
3.4.13.23 S-benzyl-L-Cys-Gly + H2O
-
Corynebacterium striatum S-benzyl-L-Cys + glycine
-
?

Subunits

EC Number Subunits Comment Organism
3.4.13.23 ? x * 50000, SDS-PAGE Corynebacterium striatum

Synonyms

EC Number Synonyms Comment Organism
3.4.13.23 thiol precursor dipeptidase
-
Corynebacterium striatum
3.4.13.23 tpdA
-
Corynebacterium striatum

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.4.13.23 0.015
-
pH 7.0, temperature not specified in the publication Corynebacterium striatum 1,10-phenanthroline
3.4.13.23 0.015
-
pH 7.0, temperature not specified in the publication Corynebacterium striatum pyridine-2,6-dicarboxylic acid

General Information

EC Number General Information Comment Organism
3.4.13.23 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 Corynebacterium striatum