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Literature summary extracted from

  • Dupourque, D.; Newton, W.A.; Snell, E.E.
    Purification and properties of D-serine dehydrase from Escherichia coli (1966), J. Biol. Chem., 241, 1233-1238.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.1.18
-
Escherichia coli

General Stability

EC Number General Stability Organism
4.3.1.18 resolved completely by dialysis against L-Cys or D-Cys, reactivated by addition of pyridoxal 5'-phosphate Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.18 O-methylserine competitive Escherichia coli
4.3.1.18 Tris inactivation is prevented by the presence of sufficient K+ or NH4+ and less effectively by Na+ or pyridoxal 5'-phosphate Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.18 1.3
-
D-Ser
-
Escherichia coli
4.3.1.18 3.2
-
D-Thr
-
Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.18 40000
-
sucrose density gradient centrifugation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.18 Escherichia coli
-
constitutive mutant
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.18
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.18 D-serine
-
Escherichia coli pyruvate + NH3
-
?
4.3.1.18 D-threonine
-
Escherichia coli 2-oxobutanoate + NH3
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.18 7.8 8
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.3.1.18 6.5 9 pH 6.5: about 30% of maximal activity, pH 9.0: about 60% of maximal activity Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.18 pyridoxal 5'-phosphate enzyme linked cofactor Escherichia coli