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Literature summary for 4.3.1.17 extracted from

  • Farias, M.E.; Strasser de Saad, A.M.; Pesce de Ruiz Holgado, A.A.; Oliver, G.
    Purification and properties of L-serine dehydratase from Lactobacillus fermentum ATCC 14931 (1991), Curr. Microbiol., 22, 205-211.
No PubMed abstract available
Search for more literature for 4.3.1.17

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
65
-
 L-Ser
-
 Limosilactobacillus fermentum

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Limosilactobacillus fermentum
Fe2+ Km: 0.55 mM Limosilactobacillus fermentum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 4 * 40000, SDS-PAGE Limosilactobacillus fermentum
150000
-
 gel filtration Limosilactobacillus fermentum

Organism

Organism UniProt Comment Textmining
Limosilactobacillus fermentum
-
 ATCC 14931
-

Purification (Commentary)

Purification (Comment) Organism
-
 Limosilactobacillus fermentum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.649
-
-
 Limosilactobacillus fermentum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
 Limosilactobacillus fermentum pyruvate + NH3
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 40000, SDS-PAGE Limosilactobacillus fermentum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Limosilactobacillus fermentum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Limosilactobacillus fermentum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate prosthetic group Limosilactobacillus fermentum
pyridoxal 5'-phosphate pyridoxal-5'-phosphate-independent enzyme Limosilactobacillus fermentum