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Literature summary extracted from

  • Szebenyi, D.M.; Musayev, F.N.; di Salvo, M.L.; Safo, M.K.; Schirch, V.
    Serine hydroxymethyltransferase: role of Glu75 and evidence that serine is cleaved by a retroaldol mechanism (2004), Biochemistry, 43, 6865-6876.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.1 hanging-drop vapour diffusion technique. Crystals of both mutants, E75L and E75Q are obtained by mixing 0.003v ml of an enzyme solution (34-44 mg/ml in 20 mM potassium phosphate, pH 7.3, with 1 mM dithiothreitol) with an equal volume of reservoir solution. The reservoir solution for E75L rcSHMT consists of 50 mM potassium phosphate, pH 6.6, 8.5-9.1% PEG 8000, and 100 mM KCl. For E75Q rcSHMT the reservoir solution consists of 15 mM potassium 2-(N-morpholino)ethanesulfonate, pH 6.4, 8.5-10% PEG 4000, and 30 mM KCl. Serine complexes are formed by adding 0.00025 ml of 250 mM L-serine directly to the drop Oryctolagus cuniculus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 E75L no activity with L-Ser and tetrahydrofolate. The mutant enzyme does not catalyze the formation of 5,10-methenyl-tetrahydropteroylglutamate or N5-hydroxymethylene-tetrahydropteroylglutamate Oryctolagus cuniculus
2.1.2.1 E75Q 500fold decrease in activity with L-Ser and tetrahydrofolate compared to wild-type enzyme, the KM-value for L-allothreonine is 10fold increased compared to wild-type value, the turnover-number for reaction with L-allothreonine is 4.3fold increased compared to wild-type enzyme Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 0.8
-
 L-Ser recombinant wild-type enzyme Oryctolagus cuniculus
2.1.2.1 4
-
 L-Ser mutant enzyme E75Q Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Oryctolagus cuniculus P07511
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 L-Ser + tetrahydrofolate
-
 Oryctolagus cuniculus Gly + 5,10-methylenetetrahydrofolate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 SHMT
-
 Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 0.02
-
 L-Ser mutant enzyme E75Q Oryctolagus cuniculus
2.1.2.1 10
-
 L-Ser recombinant wild-type enzyme Oryctolagus cuniculus