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Literature summary for 1.3.1.84 extracted from

  • Asao, M.; Alber, B.E.
    Acrylyl-coenzyme A reductase, an enzyme involved in the assimilation of 3-hydroxypropionate by Rhodobacter sphaeroides (2013), J. Bacteriol., 195, 4716-4725.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.84

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Escherichia coli
ATP dependent on Ruegeria pomeroyi

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta2 (DE3) cells Escherichia coli
expressed in Escherichia coli Rosetta2 (DE3) cells Cereibacter sphaeroides
expressed in Escherichia coli Rosetta2 (DE3) cells Ruegeria pomeroyi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0011
-
 acrylyl-CoA at pH 7.0 and 30°C Escherichia coli
0.0015
-
 acrylyl-CoA at pH 7.0 and 30°C Cereibacter sphaeroides
0.0028
-
 acrylyl-CoA at pH 7.0 and 30°C Ruegeria pomeroyi
0.018
-
 NADPH at pH 7.0 and 30°C Ruegeria pomeroyi
0.028
-
 NADPH at pH 7.0 and 30°C Cereibacter sphaeroides
0.033
-
 NADPH at pH 7.0 and 30°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Escherichia coli
Mg2+ dependent on Cereibacter sphaeroides
Mg2+ dependent on Ruegeria pomeroyi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
 2 * 37000, SDS-PAGE Escherichia coli
37000
-
 2 * 37000, SDS-PAGE Cereibacter sphaeroides
37000
-
 2 * 37000, SDS-PAGE Ruegeria pomeroyi
56000
-
 gel filtration Escherichia coli
62000
-
 gel filtration Ruegeria pomeroyi
64000
-
 gel filtration Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acrylyl-CoA + NADPH + H+ Escherichia coli
-
 propionyl-CoA + NADP+
-
 ?
acrylyl-CoA + NADPH + H+ Cereibacter sphaeroides
-
 propionyl-CoA + NADP+
-
 ?
acrylyl-CoA + NADPH + H+ Ruegeria pomeroyi
-
 propionyl-CoA + NADP+
-
 ?
acrylyl-CoA + NADPH + H+ Cereibacter sphaeroides DSM 158
-
 propionyl-CoA + NADP+
-
 ?
additional information Escherichia coli the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
additional information Cereibacter sphaeroides the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
additional information Ruegeria pomeroyi the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
additional information Escherichia coli the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?
additional information Cereibacter sphaeroides the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?
additional information Ruegeria pomeroyi the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?
additional information Cereibacter sphaeroides DSM 158 the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
additional information Cereibacter sphaeroides DSM 158 the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q3J6K9
-
-
Cereibacter sphaeroides DSM 158 Q3J6K9
-
-
Escherichia coli
-
-
-
Ruegeria pomeroyi Q5LS56
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superose 12 gel filtration Escherichia coli
Ni-NTA column chromatography and Superose 12 gel filtration Cereibacter sphaeroides
Ni-NTA column chromatography and Superose 12 gel filtration Ruegeria pomeroyi

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12
-
 cell extract, at pH 7.0 and 30°C Escherichia coli
12
-
 cell extract, at pH 7.0 and 30°C Cereibacter sphaeroides
23
-
 cell extract, at pH 7.0 and 30°C Ruegeria pomeroyi
72
-
 after 6fold purification, at pH 7.0 and 30°C Escherichia coli
98
-
 after 4fold purification, at pH 7.0 and 30°C Ruegeria pomeroyi
130
-
 after 11fold purification, at pH 7.0 and 30°C Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acrylyl-CoA + NADPH + H+
-
 Escherichia coli propionyl-CoA + NADP+
-
 ?
acrylyl-CoA + NADPH + H+
-
 Cereibacter sphaeroides propionyl-CoA + NADP+
-
 ?
acrylyl-CoA + NADPH + H+
-
 Ruegeria pomeroyi propionyl-CoA + NADP+
-
 ?
acrylyl-CoA + NADPH + H+
-
 Cereibacter sphaeroides DSM 158 propionyl-CoA + NADP+
-
 ?
additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Escherichia coli ?
-
 ?
additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Cereibacter sphaeroides ?
-
 ?
additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Ruegeria pomeroyi ?
-
 ?
additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Escherichia coli ?
-
 ?
additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Cereibacter sphaeroides ?
-
 ?
additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Ruegeria pomeroyi ?
-
 ?
additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Cereibacter sphaeroides DSM 158 ?
-
 ?
additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Cereibacter sphaeroides DSM 158 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 37000, SDS-PAGE Escherichia coli
homodimer 2 * 37000, SDS-PAGE Cereibacter sphaeroides
homodimer 2 * 37000, SDS-PAGE Ruegeria pomeroyi

Synonyms

Synonyms Comment Organism
acrylyl-CoA reductase
-
 Escherichia coli
acrylyl-CoA reductase
-
 Cereibacter sphaeroides
acrylyl-CoA reductase
-
 Ruegeria pomeroyi
acrylyl-coenzyme A reductase
-
 Escherichia coli
acrylyl-coenzyme A reductase
-
 Cereibacter sphaeroides
acrylyl-coenzyme A reductase
-
 Ruegeria pomeroyi
AcuI
-
 Escherichia coli
AcuI
-
 Cereibacter sphaeroides
AcuI
-
 Ruegeria pomeroyi

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
45
-
 acrylyl-CoA at pH 7.0 and 30°C Escherichia coli
60
-
 acrylyl-CoA at pH 7.0 and 30°C Ruegeria pomeroyi
80
-
 acrylyl-CoA at pH 7.0 and 30°C Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Cereibacter sphaeroides
NADPH the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Escherichia coli
NADPH the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Cereibacter sphaeroides
NADPH the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Ruegeria pomeroyi