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Literature summary for 2.3.1.16 extracted from

  • Pantazaki, A.A.; Ioannou, A.K.; Kyriakidis, D.A.
    A thermostable beta-ketothiolase of polyhydroxyalkanoates (PHAs) in Thermus thermophilus: purification and biochemical properties (2005), Mol. Cell. Biochem., 269, 27-36.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP activates Thermus thermophilus
NADH activates Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
acetoacetyl-CoA substrate inhibition at high concentrations Thermus thermophilus
NEM inhibition at 1 mM in absence or presence of 0.5 mM acetyl-CoA Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Thermus thermophilus
0.011
-
acetyl-CoA pH 8.0, 65°C Thermus thermophilus
0.025
-
CoA pH 8.0, 65°C Thermus thermophilus
0.025
-
acetoacetyl-CoA pH 8.0, 65°C Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Thermus thermophilus
Mg2+ activates Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45500
-
4 * 45500, SDS-PAGE Thermus thermophilus
182000
-
gel filtration Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + H2O Thermus thermophilus
-
acetate + CoA
-
r
acetyl-CoA + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
acetate + CoA
-
r
additional information Thermus thermophilus first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview ?
-
?
additional information Thermus thermophilus HB8 / ATCC 27634 / DSM 579 first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 386.4fold to homogeneity by anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, and gel filtration Thermus thermophilus

Reaction

Reaction Comment Organism Reaction ID
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA ping-pong mechanism, a cysteine residue in involved in the active site Thermus thermophilus

Renatured (Commentary)

Renatured (Comment) Organism
in situ renaturation of the enzyme from the SDS-polyacrylamide gel, after solubilization, SDS removal and denaturation with 6 M guanidine hydrochloride, overview Thermus thermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1082
-
purified enzyme Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + H2O
-
Thermus thermophilus acetate + CoA
-
r
acetyl-CoA + H2O
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 acetate + CoA
-
r
coenzyme A + acetoacetyl-CoA
-
Thermus thermophilus 2 acetyl-CoA
-
?
coenzyme A + acetoacetyl-CoA
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 2 acetyl-CoA
-
?
additional information first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview Thermus thermophilus ?
-
?
additional information first enzyme of the most common biosynthetic pathway for polyhydroxyalkanoates, overview Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 45500, SDS-PAGE Thermus thermophilus

Synonyms

Synonyms Comment Organism
beta-ketothiolase
-
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
for both reaction directions Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
15 min, purified enzyme, completely stable Thermus thermophilus
100
-
15 min, purified enzyme, loss of 23% of activity Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
for both reaction directions Thermus thermophilus