Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.3.14 extracted from

  • Helmkamp, G.H.; Bloch, K.
    beta-Hydroxydecanoyl thioester dehydrase. Studies on molecular structure and active site (1969), J. Biol. Chem., 244, 6014-6022.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-decynoyl-N-acetylcysteamine covalent modification of ative site residue H70 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-value gradually decreases with decreasing pH-value Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
2 * 18000, SDS-PAGE Escherichia coli
36000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cis-3-decenoyl-N-acetylcysteamine
-
Escherichia coli trans-2-decenoyl-N-acetylcysteamine
-
r

Subunits

Subunits Comment Organism
dimer 2 * 18000, SDS-PAGE Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
15
-
cis-3-decenoyl-N-acetylcysteamine pH 9.0, 30°C Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.3 10.2 more than 50% of activity maximum within this range Escherichia coli