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

BRENDA support

Literature summary for 1.3.1.95 extracted from

  • Teufel, R.; Kung, J.; Kockelkorn, D.; Alber, B.; Fuchs, G.
    3-Hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales (2009), J. Bacteriol., 191, 4572-4581.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.95

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta 2 (DE3) cells Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 acryloyl-CoA apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C Sulfurisphaera tokodaii
0.01
-
 acryloyl-CoA apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C Metallosphaera sedula
0.036
-
 NADPH apparent value, recombinant enzyme, at pH 7.5 and 22°C Metallosphaera sedula
0.036
-
 acryloyl-CoA apparent value, recombinant enzyme, at pH 7.5 and 22°C Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains 0.8 mol of Zn2+ per mol of enzyme monomer Sulfurisphaera tokodaii
Zn2+ contains 0.8 mol of Zn2+ per mol of enzyme monomer Metallosphaera sedula

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
 calculated from amino acid sequence Sulfurisphaera tokodaii
40000
-
 1 * 40000, SDS-PAGE Sulfurisphaera tokodaii
40000
-
 1 * 40000, SDS-PAGE Metallosphaera sedula
43000
-
 gel filtration Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Metallosphaera sedula
-
-
-
Sulfurisphaera tokodaii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
heat precipitation and Ni2+-chelating Sepharose column chromatography Sulfurisphaera tokodaii
heat precipitation, Q Sepharose column chromatography, carboxymethylcellulose column chromatography, ammonium sulfate precipitation, phenyl-Sepharose column chromatography, and Resource-S gel filtration Metallosphaera sedula

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.014
-
 cell extract, at pH 7.5 and 22°C Metallosphaera sedula
2.9
-
 after 210fold purification, at pH 7.5 and 22°C Metallosphaera sedula
4.6
-
 cell extract, at pH 7.5 and 22°C Sulfurisphaera tokodaii
18.7
-
 after 4.1fold purification, at pH 7.5 and 22°C Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acryloyl-CoA + NADPH + H+
-
 Metallosphaera sedula propanoyl-CoA + NADP+
-
 ir
acryloyl-CoA + NADPH + H+ 100% specificity Sulfurisphaera tokodaii propanoyl-CoA + NADP+
-
 ir
additional information less than 1% specificity for crotonyl-CoA Sulfurisphaera tokodaii ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 40000, SDS-PAGE Sulfurisphaera tokodaii
monomer 1 * 40000, SDS-PAGE Metallosphaera sedula

Synonyms

Synonyms Comment Organism
acryloyl-CoA reductase
-
 Sulfurisphaera tokodaii
acryloyl-CoA reductase
-
 Metallosphaera sedula
acryloyl-CoA reductase (NADPH)
-
 Sulfurisphaera tokodaii
acryloyl-CoA reductase (NADPH)
-
 Metallosphaera sedula
acryloyl-coenzyme A reductase
-
 Sulfurisphaera tokodaii
acryloyl-coenzyme A reductase
-
 Metallosphaera sedula

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13
-
 acryloyl-CoA apparent value, recombinant enzyme, at pH 7.5 and 22°C Sulfurisphaera tokodaii
13
-
 acryloyl-CoA apparent value, recombinant enzyme, at pH 7.5 and 22°C Metallosphaera sedula

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Sulfurisphaera tokodaii

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Sulfurisphaera tokodaii
FAD
-
 Metallosphaera sedula
NADPH
-
 Sulfurisphaera tokodaii
NADPH
-
 Metallosphaera sedula