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Literature summary extracted from

  • Craig, P.A.; Dekker, E.E.
    The sulfhydryl content of L-threonine dehydrogenase from Escherichia coli K-12: relation to catalytic activity and Mn2+ activation (1990), Biochim. Biophys. Acta, 1037, 30-38.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.103 iodoacetamide 3.2 mM, 10% inhibition Escherichia coli K-12
1.1.1.103 iodoacetate 15% protection against inhibition with 5 mM NAD+, 30% with 5 mM L-threonine, 60-70% protection in the presence of both NAD+ and L-threonine, inactivation occurs more rapidly in the presence of Cd2+; enzyme contains 6 half-cystine residues per subunit, 2 disulfide bonds and 4 sulfhydryl groups Escherichia coli K-12
1.1.1.103 methylmethanethiosulfonate 0.4 mM, 350fold molar excess over enzyme sulfhydryl groups leads to complete inactivation Escherichia coli K-12
1.1.1.103 p-mercuribenzoate 10fold excess leads to immidiate inactivation Escherichia coli K-12
1.1.1.103 thionitrobenzoate 40fold molar excess, gradual 99% loss of enzyme activity Escherichia coli K-12

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.103 Cd2+ activation is not thiol-dependent Escherichia coli K-12

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.103 L-threonine + NAD+ Escherichia coli K-12
-
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.103 Escherichia coli K-12
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.103 L-threonine + NAD+
-
Escherichia coli K-12 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.103 NAD+
-
Escherichia coli K-12