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Literature summary 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

Activating Compound

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

Cloned(Commentary)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.84 0.0011
-
 acrylyl-CoA at pH 7.0 and 30°C Escherichia coli
1.3.1.84 0.0015
-
 acrylyl-CoA at pH 7.0 and 30°C Cereibacter sphaeroides
1.3.1.84 0.0028
-
 acrylyl-CoA at pH 7.0 and 30°C Ruegeria pomeroyi
1.3.1.84 0.018
-
 NADPH at pH 7.0 and 30°C Ruegeria pomeroyi
1.3.1.84 0.028
-
 NADPH at pH 7.0 and 30°C Cereibacter sphaeroides
1.3.1.84 0.033
-
 NADPH at pH 7.0 and 30°C Escherichia coli

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.84 37000
-
 2 * 37000, SDS-PAGE Escherichia coli
1.3.1.84 37000
-
 2 * 37000, SDS-PAGE Cereibacter sphaeroides
1.3.1.84 37000
-
 2 * 37000, SDS-PAGE Ruegeria pomeroyi
1.3.1.84 56000
-
 gel filtration Escherichia coli
1.3.1.84 62000
-
 gel filtration Ruegeria pomeroyi
1.3.1.84 64000
-
 gel filtration Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.84 acrylyl-CoA + NADPH + H+ Escherichia coli
-
 propionyl-CoA + NADP+
-
 ?
1.3.1.84 acrylyl-CoA + NADPH + H+ Cereibacter sphaeroides
-
 propionyl-CoA + NADP+
-
 ?
1.3.1.84 acrylyl-CoA + NADPH + H+ Ruegeria pomeroyi
-
 propionyl-CoA + NADP+
-
 ?
1.3.1.84 acrylyl-CoA + NADPH + H+ Cereibacter sphaeroides DSM 158
-
 propionyl-CoA + NADP+
-
 ?
1.3.1.84 additional information Escherichia coli the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
1.3.1.84 additional information Cereibacter sphaeroides the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
1.3.1.84 additional information Ruegeria pomeroyi the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH ?
-
 ?
1.3.1.84 additional information Escherichia coli the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?
1.3.1.84 additional information Cereibacter sphaeroides the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?
1.3.1.84 additional information Ruegeria pomeroyi the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?
1.3.1.84 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 ?
-
 ?
1.3.1.84 additional information Cereibacter sphaeroides DSM 158 the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate ?
-
 ?

Organism

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.84 12
-
 cell extract, at pH 7.0 and 30°C Escherichia coli
1.3.1.84 12
-
 cell extract, at pH 7.0 and 30°C Cereibacter sphaeroides
1.3.1.84 23
-
 cell extract, at pH 7.0 and 30°C Ruegeria pomeroyi
1.3.1.84 72
-
 after 6fold purification, at pH 7.0 and 30°C Escherichia coli
1.3.1.84 98
-
 after 4fold purification, at pH 7.0 and 30°C Ruegeria pomeroyi
1.3.1.84 130
-
 after 11fold purification, at pH 7.0 and 30°C Cereibacter sphaeroides

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.84 acrylyl-CoA + NADPH + H+
-
 Escherichia coli propionyl-CoA + NADP+
-
 ?
1.3.1.84 acrylyl-CoA + NADPH + H+
-
 Cereibacter sphaeroides propionyl-CoA + NADP+
-
 ?
1.3.1.84 acrylyl-CoA + NADPH + H+
-
 Ruegeria pomeroyi propionyl-CoA + NADP+
-
 ?
1.3.1.84 acrylyl-CoA + NADPH + H+
-
 Cereibacter sphaeroides DSM 158 propionyl-CoA + NADP+
-
 ?
1.3.1.84 additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Escherichia coli ?
-
 ?
1.3.1.84 additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Cereibacter sphaeroides ?
-
 ?
1.3.1.84 additional information the enzyme is highly specific for NADPH with catalytic efficiencies of more than 10fold higher for NADPH than for NADH Ruegeria pomeroyi ?
-
 ?
1.3.1.84 additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Escherichia coli ?
-
 ?
1.3.1.84 additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Cereibacter sphaeroides ?
-
 ?
1.3.1.84 additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Ruegeria pomeroyi ?
-
 ?
1.3.1.84 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 ?
-
 ?
1.3.1.84 additional information the enzyme shows less than 1% activity with crotonyl-CoA, 3-hydroxypropionyl-CoA and acrylate Cereibacter sphaeroides DSM 158 ?
-
 ?

Subunits

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

Synonyms

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.84 45
-
 acrylyl-CoA at pH 7.0 and 30°C Escherichia coli
1.3.1.84 60
-
 acrylyl-CoA at pH 7.0 and 30°C Ruegeria pomeroyi
1.3.1.84 80
-
 acrylyl-CoA at pH 7.0 and 30°C Cereibacter sphaeroides

Cofactor

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