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Literature summary for 4.3.1.17 extracted from

  • Gannon, F.; Bridgeland, E.S.; Jones, K.M.
    L-Serine dehydratase from Arthrobacter globiformis (1977), Biochem. J., 161, 345-355.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
D-Ser competitive Arthrobacter globiformis
HgCl2
-
Arthrobacter globiformis
L-Cys competitive Arthrobacter globiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7
-
L-Ser
-
Arthrobacter globiformis

Metals/Ions

Metals/Ions Comment Organism Structure
KCl nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity is produced with 22.5 mM KCl Arthrobacter globiformis
MgCl2 nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity with 1.0 mM MgCl2 Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Arthrobacter globiformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
660
-
-
Arthrobacter globiformis

Storage Stability

Storage Stability Organism
-20°C, pH 7.0-8.0, stable over many months, enzyme in crude extract Arthrobacter globiformis
-70°C, 0.6 mg/ml protein, 30% loss of activity after 1 month, purified enzyme Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine specific for L-Ser Arthrobacter globiformis pyruvate + NH3
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
Arthrobacter globiformis