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Literature summary for 4.3.1.16 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

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
T62
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas sp.

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

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