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Literature summary for 4.3.1.18 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
Search for more literature for 4.3.1.18

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
O-methylserine competitive Escherichia coli
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 constitutive mutant
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8 8
-
 Escherichia coli

pH Range

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

Cofactor

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