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Literature summary extracted from

  • Hofmeister, A.E.M.; Grabowski, R.; Linder, D.; Buckel, W.
    L-Serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups (1993), Eur. J. Biochem., 215, 341-349.
    View publication on PubMed

General Stability

EC Number General Stability Organism
4.3.1.17 extreme instability does not permit purification to homogeneity Anaerotignum propionicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.17 D-Ser
-
 Anaerotignum propionicum
4.3.1.17 L-Cys
-
 Anaerotignum propionicum
4.3.1.19 hydroxylamine
-
 Anaerotignum propionicum
4.3.1.19 NaBH4
-
 Anaerotignum propionicum
4.3.1.19 phenylhydrazine reversed by pyridoxal 5'-phosphate Anaerotignum propionicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.17 5
-
 L-Ser
-
 Anaerotignum propionicum
4.3.1.19 7.7
-
 L-Thr
-
 Anaerotignum propionicum
4.3.1.19 380
-
 L-Ser
-
 Anaerotignum propionicum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.1.17 Iron iron-sulfur-dependent enzyme Anaerotignum propionicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.17 10000
-
 1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE Anaerotignum propionicum
4.3.1.17 26000
-
 1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE Anaerotignum propionicum
4.3.1.17 26000
-
 4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE Anaerotignum propionicum
4.3.1.17 30000
-
 4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE Anaerotignum propionicum
4.3.1.17 57000
-
 gel filtration in presence of 10 mM Fe2+, dimeric enzyme form Anaerotignum propionicum
4.3.1.17 230000
-
 gel filtration in absence of Fe2+, octameric enzyme form Anaerotignum propionicum
4.3.1.19 39000
-
 4 * 39000, SDS-PAGE Anaerotignum propionicum
4.3.1.19 160000
-
 gel filtration Anaerotignum propionicum

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.17 Anaerotignum propionicum
-
-
-
4.3.1.19 Anaerotignum propionicum
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
4.3.1.17 rapid loss of activity upon exposure to air, reactivation by Fe2+ Anaerotignum propionicum

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.17 partial Anaerotignum propionicum
4.3.1.19
-
 Anaerotignum propionicum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.17 additional information
-
-
 Anaerotignum propionicum
4.3.1.19 additional information
-
-
 Anaerotignum propionicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.17 L-serine
-
 Anaerotignum propionicum pyruvate + NH3
-
 ?
4.3.1.19 L-Ser
-
 Anaerotignum propionicum pyruvate + NH3
-
 ?
4.3.1.19 L-threonine
-
 Anaerotignum propionicum 2-oxobutanoate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.1.17 dimer 1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE Anaerotignum propionicum
4.3.1.17 octamer 4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE Anaerotignum propionicum
4.3.1.19 tetramer 4 * 39000, SDS-PAGE Anaerotignum propionicum

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.17 pyridoxal 5'-phosphate pyridoxal-5'-phosphate-independent enzyme Anaerotignum propionicum
4.3.1.19 pyridoxal 5'-phosphate required Anaerotignum propionicum