Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea . The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA . Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+.
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SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:NADP+ oxidoreductase
Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA [2]. Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+.
the purified proteins of malonyl-CoA reductase (MCR) and 3-hydroxypropionyl-CoA dehydratase (3HPCD) from Sulfolobus tokodaii, and the proteins of malonate semialdehyde reductase (MSR), 3-hydroxypropionyl-CoA synthetase (3HPCS), and acryloyl-CoA reductase (ACR) from Metallosphaera sedula are used to convert malonyl-CoA to propionyl-CoA in vitro. Malonyl-CoA is almost completely converted to propionyl-CoA even at 23°C, and no other acyl-CoA products are detected, indicating that this system is robust. The turnover rate of this pathway is 37/min at 37°C
the purified proteins of malonyl-CoA reductase (MCR) and 3-hydroxypropionyl-CoA dehydratase (3HPCD) from Sulfolobus tokodaii, and the proteins of malonate semialdehyde reductase (MSR), 3-hydroxypropionyl-CoA synthetase (3HPCS), and acryloyl-CoA reductase (ACR) from Metallosphaera sedula are used to convert malonyl-CoA to propionyl-CoA in vitro. Malonyl-CoA is almost completely converted to propionyl-CoA even at 23°C, and no other acyl-CoA products are detected, indicating that this system is robust. The turnover rate of this pathway is 37/min at 37°C
the purified proteins of malonyl-CoA reductase (MCR) and 3-hydroxypropionyl-CoA dehydratase (3HPCD) from Sulfolobus tokodaii, and the proteins of malonate semialdehyde reductase (MSR), 3-hydroxypropionyl-CoA synthetase (3HPCS), and acryloyl-CoA reductase (ACR) from Metallosphaera sedula are used to convert malonyl-CoA to propionyl-CoA in vitro. Malonyl-CoA is almost completely converted to propionyl-CoA even at 23°C, and no other acyl-CoA products are detected, indicating that this system is robust. The turnover rate of this pathway is 37/min at 37°C
the partially purified recombinant protein has activity of acryloyl-CoA reductase but not 3-hydroxypropionyl-CoA reductase. The 3-hydroxypropionyl-CoA reductase activity observed in cell extracts results from the coupling of the acryloyl-CoA hydratase with an acryloyl-CoA reductase activity
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
Ruegeria pomeroyi DSS-3 possesses two general pathways for metabolism of dimethylsulphoniopropionate (DMSP), an osmolyte of algae and abundant carbon source for marine bacteria. In the DMSP cleavage pathway, acrylate is transformed into acryloyl-CoA by propionate-CoA ligase (SPO2934) and other unidentified acyl-CoA ligases. Acryloyl-CoA is then reduced to propionyl-CoA by AcuI or SPO1914. Acryloyl-CoA is also rapidly hydrated to 3-hydroxypropionyl-CoA by acryloyl-CoA hydratase (SPO0147)
the enzyme is part of the 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle fixes CO2 in extremely thermoacidophilic archaea, pathway regulation and modeling, enzyme kinetics-based models, reaction kinetics model of the 3HP/4HB cycle, detailed overview
the enzyme is part of the 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle fixes CO2 in extremely thermoacidophilic archaea, pathway regulation and modeling, enzyme kinetics-based models, reaction kinetics model of the 3HP/4HB cycle, detailed overview
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
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
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
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
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
to construct an acrylic acid-producing pathway in Escherichia coli strain MG1655DELTArecADELTAendA(DE3)/pZL42, heterologous expression of malonyl-CoA reductase (MCR), malonate semialdehyde reductase (MSR), 3-hydroxypropionyl-CoA synthetase (3HPCS), and 3-hydroxypropionyl-CoA dehydratase (3HPCD) Metallosphaera sedula is accompanied by recombinant overexpression of succinyl-CoA synthetase (SCS) from Escherichia coli. The engineered strain produces 13.28 mg/l of acrylic acid. To construct a propionic acid-producing pathway, the same five genes are expressed, with the addition of Metallosphaera sedula acryloyl-CoA reductase (ACR). The engineered strain produces 1430 mg/l of propionic acid, detailed overview
to construct an acrylic acid-producing pathway in Escherichia coli strain MG1655DELTArecADELTAendA(DE3)/pZL42, heterologous expression of malonyl-CoA reductase (MCR), malonate semialdehyde reductase (MSR), 3-hydroxypropionyl-CoA synthetase (3HPCS), and 3-hydroxypropionyl-CoA dehydratase (3HPCD) Metallosphaera sedula is accompanied by recombinant overexpression of succinyl-CoA synthetase (SCS) from Escherichia coli. The engineered strain produces 13.28 mg/l of acrylic acid. To construct a propionic acid-producing pathway, the same five genes are expressed, with the addition of Metallosphaera sedula acryloyl-CoA reductase (ACR). The engineered strain produces 1430 mg/l of propionic acid, detailed overview
to construct an acrylic acid-producing pathway in Escherichia coli strain MG1655DELTArecADELTAendA(DE3)/pZL42, heterologous expression of malonyl-CoA reductase (MCR), malonate semialdehyde reductase (MSR), 3-hydroxypropionyl-CoA synthetase (3HPCS), and 3-hydroxypropionyl-CoA dehydratase (3HPCD) Metallosphaera sedula is accompanied by recombinant overexpression of succinyl-CoA synthetase (SCS) from Escherichia coli. The engineered strain produces 13.28 mg/l of acrylic acid. To construct a propionic acid-producing pathway, the same five genes are expressed, with the addition of Metallosphaera sedula acryloyl-CoA reductase (ACR). The engineered strain produces 1430 mg/l of propionic acid, detailed overview
construction of a gene SPO1914 disruption mutant by homologous recombination of suicide plasmids, the mutant is unable to grow on acrylate as the sole carbon source
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange and hydrophobic interaction chromatography, ultrafiltration, hydroxyapatatite chromatography, and again ultrafiltration. The enzyme is separated from acryloyl-CoA hydratase
gene Msed_1426, cloned from genomic DNA, recombinant co-expression of His-tagged enzyme with enzyme succinic semialdehyde reductase (NADPH), SSR, gene Msed_1424 from Metallosphaera sedula, in Escherichia coli strain Rosetta 2(DE3). Construction of a yeast two-hybrid assay for protein interaction analysis of ACR and SSR. ACR cannot be expressed in soluble, active form in Escherichia coli
gene SPO1914, the gene is adjacent to and predicted to be within the same transcriptional unit as dmdA, which encodes the enzyme for the first step of the demethylation pathway
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
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
successful reconstitution a portion of the 3-hydroxypropionate/4-hydroxybutyrate cycle from Metallosphaera sedula in Escherichia coli to produce acrylic acid and propionic acid, involving the acryloyl-CoA reductase (ACR), overview
successful reconstitution a portion of the 3-hydroxypropionate/4-hydroxybutyrate cycle from Metallosphaera sedula in Escherichia coli to produce acrylic acid and propionic acid, involving the acryloyl-CoA reductase (ACR), overview
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
Production of acrylic acid and propionic acid by constructing a portion of the 3-hydroxypropionate/4-hydroxybutyrate cycle from Metallosphaera sedula in Escherichia coli