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Literature summary for 4.2.3.1 extracted from

  • Morneau, D.J.; Abouassaf, E.; Skanes, J.E.; Aitken, S.M.
    Development of a continuous assay and steady-state characterization of Escherichia coli threonine synthase (2012), Anal. Biochem., 423, 78-85.
    View publication on PubMed
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Application

Application Comment Organism
analysis continuous, coupled spectrophotometric threonine synthase assay. The sequential actions of threonine deaminase and hydroxyisocaproate dehydrogenase convert the L-Thr product of TS to alpha-ketobutyrate and then to 2-hydroxybutyrate, respectively, and are monitored as the decrease in absorbance at 340 nm resulting from the concomitant oxidation of beta-nicotinamide adenine dinucleotide to NAD+ by hydroxyisocaproate dehydrogenase Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.34
-
 O-phospho-L-homoserine pH 8.0, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-L-homoserine + H2O
-
 Escherichia coli L-threonine + phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4
-
 O-phospho-L-homoserine pH 8.0, 25°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.7
-
-
 Escherichia coli