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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

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
gene RSP_1434, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3) Cereibacter sphaeroides
gene SPO_1914, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), recombinant expression in Rhodobacter sphaeroides mutant DELTAacuI::kan complements 3-hydroxypropionate-dependent growth of the mutant strain Ruegeria pomeroyi
gene yhdH, cloning and expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), recombinant expression in Rhodobacter sphaeroides mutant DELTAacuI::kan complements 3-hydroxypropionate-dependent growth of the mutant strain Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of mutant DELTAacuI::kan. The introduction of codon-optimized genes SPO_1914 or yhdH into the DELTAacuI::kan mutant of Rhodobacter sphaeroides on plasmid pMA5-1 complements 3-hydroxypropionate-dependent growth of the mutant strain Cereibacter sphaeroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Cereibacter sphaeroides
additional information
-
additional information Michaelis-Menten kinetics Ruegeria pomeroyi
additional information
-
additional information Michaelis-Menten kinetics Escherichia coli
0.0011
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Escherichia coli
0.0015
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Cereibacter sphaeroides
0.0028
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Ruegeria pomeroyi
0.018
-
NADPH pH 7.0, 30┬░C, recombinant His-tagged enzyme Ruegeria pomeroyi
0.028
-
NADPH pH 7.0, 30┬░C, recombinant His-tagged enzyme Cereibacter sphaeroides
0.033
-
NADPH pH 7.0, 30┬░C, recombinant His-tagged enzyme Escherichia coli

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
recombinant His10-tagged enzyme, gel filtration Escherichia coli
62000
-
recombinant His10-tagged enzyme, gel filtration Ruegeria pomeroyi
64000
-
recombinant His10-tagged enzyme, 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+ Cereibacter sphaeroides
-
propanoyl-CoA + NADP+
-
?
acrylyl-CoA + NADPH + H+ Ruegeria pomeroyi
-
propanoyl-CoA + NADP+
-
?
acrylyl-CoA + NADPH + H+ Escherichia coli
-
propanoyl-CoA + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q3J6K9
-
-
Escherichia coli P26646 substrain MG1655
-
Ruegeria pomeroyi Q5LS56
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His10-tagged enzyme 11fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration Cereibacter sphaeroides
recombinant His10-tagged enzyme 4fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration Ruegeria pomeroyi
recombinant His10-tagged enzyme 6fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining
additional information anoxygenic phototroph Rhodobacter sphaeroides uses 3-hydroxypropionate as a sole carbon source for growth Cereibacter sphaeroides
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
72
-
pH 7.0, 30┬░C, purified recombinant His-tagged enzyme Escherichia coli
98
-
pH 7.0, 30┬░C, purified recombinant His-tagged enzyme Ruegeria pomeroyi
130
-
pH 7.0, 30┬░C, purified recombinant His-tagged enzyme Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acrylyl-CoA + NADH + H+
-
Cereibacter sphaeroides propanoyl-CoA + NAD+
-
?
acrylyl-CoA + NADH + H+
-
Ruegeria pomeroyi propanoyl-CoA + NAD+
-
?
acrylyl-CoA + NADH + H+
-
Escherichia coli propanoyl-CoA + NAD+
-
?
acrylyl-CoA + NADPH + H+
-
Cereibacter sphaeroides propanoyl-CoA + NADP+
-
?
acrylyl-CoA + NADPH + H+
-
Ruegeria pomeroyi propanoyl-CoA + NADP+
-
?
acrylyl-CoA + NADPH + H+
-
Escherichia coli propanoyl-CoA + NADP+
-
?
additional information no activity with crotonyl-CoA. AcuI also does not catalyze reduction of acrylate or dehydration/reduction of 3-hydroxypropionyl-CoA Cereibacter sphaeroides ?
-
?
additional information the enzyme shows a low but detectable activity for NADPH-dependent crotonyl-CoA reduction Ruegeria pomeroyi ?
-
?
additional information the enzyme shows a low but detectable activity for NADPH-dependent crotonyl-CoA reduction Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 37000, about, recombinant His10-tagged enzyme, SDS-PAGE Cereibacter sphaeroides
homodimer 2 * 37000, about, recombinant His10-tagged enzyme, SDS-PAGE Ruegeria pomeroyi
homodimer 2 * 37000, about, recombinant His10-tagged enzyme, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
acrylyl-CoA reductase
-
Cereibacter sphaeroides
acrylyl-CoA reductase
-
Ruegeria pomeroyi
acrylyl-CoA reductase
-
Escherichia coli
acrylyl-coenzyme A reductase
-
Cereibacter sphaeroides
acrylyl-coenzyme A reductase
-
Ruegeria pomeroyi
acrylyl-coenzyme A reductase
-
Escherichia coli
AcuI
-
Cereibacter sphaeroides
AcuI
-
Ruegeria pomeroyi
AcuI
-
Escherichia coli
NADPH-dependent acrylyl-CoA reductase
-
Cereibacter sphaeroides
NADPH-dependent acrylyl-CoA reductase
-
Ruegeria pomeroyi
NADPH-dependent acrylyl-CoA reductase
-
Escherichia coli
RSP_1434
-
Cereibacter sphaeroides
SPO_1914
-
Ruegeria pomeroyi
yhdH
-
Escherichia coli

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
30
-
assay at Cereibacter sphaeroides
30
-
assay at Ruegeria pomeroyi
30
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
45
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Escherichia coli
60
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Ruegeria pomeroyi
80
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Cereibacter sphaeroides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 9 broad optimum Cereibacter sphaeroides
7
-
assay at Ruegeria pomeroyi
7
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information the catalytic efficiency for NADPH is 10fold higher compared to NADH Escherichia coli
additional information the catalytic efficiency for NADPH is about 70fold higher compared to NADH Ruegeria pomeroyi
additional information the catalytic efficiency for NADPH is more than 10fold higher compared to NADH Cereibacter sphaeroides
NADH low activity Cereibacter sphaeroides
NADH low activity Ruegeria pomeroyi
NADH low activity Escherichia coli
NADPH highly specific for Cereibacter sphaeroides
NADPH highly specific for Ruegeria pomeroyi
NADPH highly specific for Escherichia coli

Expression

Organism Comment Expression
Cereibacter sphaeroides the enzyme is upregulated in cell extracts of Rhodobacter sphaeroides grown with 3-hydroxypropionate compared to those grown with succinate as a sole carbon source up

General Information

General Information Comment Organism
evolution the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily Cereibacter sphaeroides
evolution the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily Ruegeria pomeroyi
evolution the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily Escherichia coli
malfunction the introduction of codon-optimized SPO_1914 or yhdH into a DELTAacuI::kan mutant of Rhodobacter sphaeroides on a plasmid complements 3-hydroxypropionate-dependent growth. But in their native hosts, SPO_1914 and yhdH are believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate. Complementation of the DELTAacuI::kan mutant phenotype by crotonyl-CoA carboxylase/reductase from Rhodobacter sphaeroides is attributed to the fact that the fact that the enzyme also uses acrylyl-CoA as a substrate Cereibacter sphaeroides
metabolism enzyme SPO_1914 is believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate Ruegeria pomeroyi
metabolism enzyme yhdH is believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate Escherichia coli
metabolism the enzyme is part of the proposed reductive pathway for 3-hydroxypropionate assimilation by Rhodobacter sphaeroides 2.4.1, overview Cereibacter sphaeroides
physiological function the enzyme is involved in 3-hydroxypropionate assimilation via the reductive conversion to propionyl-coenzyme A (CoA). Rhodobacter sphaeroides catalyzes the NADPH-dependent acrylyl-CoA reduction to produce propionyl-CoA. Reductive conversion of 3-hydroxypropionate to propionyl-CoA is a necessary route for assimilation of this C3 compound and ultimately supplies succinyl-CoA, a precursor metabolite required for cell carbon biosynthesis Cereibacter sphaeroides
physiological function the enzyme is involved in 3-hydroxypropionate assimilation via the reductive conversion to propionyl-coenzyme A (CoA). The plasmid-encoded, codon-optimized SPO_1914 enzyme, introduced of into a DELTAacuI::kan mutant of Rhodobacter sphaeroides, complements the 3-hydroxypropionate-dependent growth of the mutant Ruegeria pomeroyi
physiological function the enzyme is involved in 3-hydroxypropionate assimilation via the reductive conversion to propionyl-coenzyme A (CoA). The plasmid-encoded, codon-optimized yhdH enzyme, introduced of into a DELTAacuI::kan mutant of Rhodobacter sphaeroides, complements the 3-hydroxypropionate-dependent growth of the mutant Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
100
-
NADH pH 7.0, 30┬░C, recombinant His-tagged enzyme Ruegeria pomeroyi
270
-
NADH pH 7.0, 30┬░C, recombinant His-tagged enzyme Escherichia coli
420
-
NADH pH 7.0, 30┬░C, recombinant His-tagged enzyme Cereibacter sphaeroides
2700
-
NADPH pH 7.0, 30┬░C, recombinant His-tagged enzyme Escherichia coli
5700
-
NADPH pH 7.0, 30┬░C, recombinant His-tagged enzyme Cereibacter sphaeroides
6700
-
NADPH pH 7.0, 30┬░C, recombinant His-tagged enzyme Ruegeria pomeroyi
53333
-
acrylyl-CoA pH 7.0, 30┬░C, recombinant His-tagged enzyme Cereibacter sphaeroides