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Literature summary for 4.1.99.1 extracted from

  • Xu, Y.; Zhang, Z.; Ali, M.M.; Sauder, J.; Deng, X.; Giang, K.; Aguirre, S.D.; Pelton, R.; Li, Y.; Filipe, C.D.
    Turning tryptophanase into odor-generating biosensors (2014), Angew. Chem. Int. Ed. Engl., 53, 2620-2622 .
    View publication on PubMed

Application

Application Comment Organism
analysis the metabolic enzyme tryptophanase (TPase) is the key component in an odor-based sensor system. The enzyme is able to convert an odorless substrate like S-methyl-L-cysteine or L-tryptophan into the odorous products methyl mercaptan or indole. For biosensor construction, TPase is biotinylated so that it can be coupled with a molecular recognition element, such as an antibody, to develop an ELISA-like assay. This method is used for the detection of an antibody present in nM concentrations by the human nose. TPase can also be combined with the enzyme pyridoxal kinase (PKase) for use in a coupled assay to detect adenosine 5'-triphosphate (ATP). When ATP is present in the low mM concentration range, the coupled enzymatic system generates an odor that is easily detectable by the human nose. Biotinylated TPase can be combined with various biotin-labeled molecular recognition elements, thereby enabling a broad range of applications for this odor-based reporting system Escherichia coli

Protein Variants

Protein Variants Comment Organism
analysis the metabolic enzyme tryptophanase (TPase) is used for biosensor construction, TPase is biotinylated so that it can be coupled with a molecular recognition element, such as an antibody, to develop an ELISA-like assay. This method is used for the detection of an antibody present in nM concentrations by the human nose. TPase can also be combined with the enzyme pyridoxal kinase (PKase) for use in a coupled assay to detect adenosine 5'-triphosphate (ATP). When ATP is present in the low mM concentration range, the coupled enzymatic system generates an odor that is easily detectable by the human nose. Biotinylated TPase can be combined with various biotinlabeled molecular recognition elements, thereby enabling a broad range of applications for this odor-based reporting system Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + H2O Escherichia coli
-
indole + pyruvate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A853
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + H2O
-
Escherichia coli indole + pyruvate + NH3
-
?
S-methyl-L-cysteine + H2O
-
Escherichia coli methanethiol + pyruvate + NH3
-
?

Subunits

Subunits Comment Organism
tetramer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
Tpase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on, the activity of TPase can be modulated by the concentration of pyridoxal 5'-phosphate Escherichia coli

General Information

General Information Comment Organism
physiological function the metabolic enzyme tryptophanase (TPase) is able to convert an odorless substrate like S-methyl-L-cysteine or L-tryptophan into the odorous products methyl mercaptan or indole Escherichia coli