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Literature summary for 4.1.2.48 extracted from

  • Kim, J.; Kershner, J.P.; Novikov, Y.; Shoemaker, R.K.; Copley, S.D.
    Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis (2010), Mol. Syst. Biol., 6, 436.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.2.48

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.027
-
 L-4-hydroxythreonine pH 8.0, 25°C Escherichia coli
0.052
-
 L-allo-threonine pH 8.0, 25°C Escherichia coli
4
-
 L-threonine pH 8.0, 25°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycine + glycolaldehyde Escherichia coli low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase L-4-hydroxythreonine
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycine + glycolaldehyde low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase Escherichia coli L-4-hydroxythreonine
-
 r
L-4-hydroxythreonine cleavage of L-4-hydroxythreonine is as efficient as cleavage of L-allo-threonine Escherichia coli glycine + glycolaldehyde
-
 r
L-allo-threonine
-
 Escherichia coli glycine + acetaldehyde
-
 r
L-threonine
-
 Escherichia coli glycine + acetaldehyde
-
 r

Synonyms

Synonyms Comment Organism
LtaE
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1
-
 L-threonine pH 8.0, 25°C Escherichia coli
1.44
-
 L-4-hydroxythreonine pH 8.0, 25°C Escherichia coli
3.2
-
 L-allo-threonine pH 8.0, 25°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

General Information

General Information Comment Organism
physiological function low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.8
-
 L-threonine pH 8.0, 25°C Escherichia coli
5.3
-
 L-4-hydroxythreonine pH 8.0, 25°C Escherichia coli
6.2
-
 L-allo-threonine pH 8.0, 25°C Escherichia coli