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Literature summary extracted from

  • Wada, M.; Matsumoto, T.; Nakamori, S.; Sakamoto, M.; Kataoka, M.; Liu, J.Q.; Itoh, N.; Yamada, H.; Shimizu, S.
    Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62 (1999), FEMS Microbiol. Lett., 179, 147-151.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.16 Cu2+
-
 Pseudomonas sp.
4.3.1.16 EDTA
-
 Pseudomonas sp.
4.3.1.16 hydroxylamine
-
 Pseudomonas sp.
4.3.1.16 Zn2+
-
 Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.16 0.74
-
 L-threo-3-hydroxyaspartate
-
 Pseudomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.1.16 Ca2+ activates Pseudomonas sp.
4.3.1.16 Co2+ activates Pseudomonas sp.
4.3.1.16 Fe2+ activates Pseudomonas sp.
4.3.1.16 Mg2+ activates Pseudomonas sp.
4.3.1.16 Mn2+ activates Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.16 59000
-
 gel filtration Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.16 Pseudomonas sp.
-
 T62
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.16
-
 Pseudomonas sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.16 8
-
-
 Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.16 L-threo-3-hydroxyaspartate no substrates are D-threo or D,L-erythro-3-hydroxyaspartate Pseudomonas sp. oxaloacetate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.1.16 More SDS-PAGE analysis shows 39000 subunit, either monomer or dimer Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.16 pyridoxal 5'-phosphate
-
 Pseudomonas sp.