1.3.1.84: acrylyl-CoA reductase (NADPH)
This is an abbreviated version!
For detailed information about acrylyl-CoA reductase (NADPH), go to the full flat file.
Word Map on EC 1.3.1.84
-
1.3.1.84
-
propionyl-coa
-
acrylate
-
acuis
-
3-hydroxypropionate
-
3-hydroxypropionyl-coa
-
dehydratase
-
chloroflexus
-
sedula
-
crotonyl-coa
-
aurantiacus
-
ruegeria
-
dimethylsulfoniopropionate
-
metallosphaera
-
3-hydroxypropionate/4-hydroxybutyrate
-
hyper-sensitive
-
pomeroyi
-
lyases
-
dmdas
-
ethylmalonyl-coa
-
sphaeroides
-
roseobacters
-
succinyl-coa
-
synthesis
- 1.3.1.84
- propionyl-coa
- acrylate
-
acuis
- 3-hydroxypropionate
- 3-hydroxypropionyl-coa
- dehydratase
- chloroflexus
- sedula
- crotonyl-coa
- aurantiacus
- ruegeria
- dimethylsulfoniopropionate
- metallosphaera
-
3-hydroxypropionate/4-hydroxybutyrate
-
hyper-sensitive
- pomeroyi
- lyases
-
dmdas
- ethylmalonyl-coa
- sphaeroides
- roseobacters
- succinyl-coa
- synthesis
Reaction
Synonyms
Acr, acryloyl-CoA reductase, acryloyl-CoA reductase (NADPH), acryloyl-coenzyme A reductase, acrylyl-CoA reductase, acrylyl-coenzyme A reductase, AcuI, Msed_1426, NADPH-dependent acryloyl-CoA reductase activity, NADPH-dependent acrylyl-CoA reductase, RSP_1434, SPO1914, SPO_1914, yhdH
ECTree
Advanced search results
General Information
General Information on EC 1.3.1.84 - acrylyl-CoA reductase (NADPH)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily
evolution
the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily
evolution
the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily
a SPO1914 mutant is unable to grow on acrylate as the sole carbon source, supporting its role in the dimethylsulphoniopropionate assimilation pathway
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
enzyme SPO_1914 is believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate
metabolism
enzyme yhdH is believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate
metabolism
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)
metabolism
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
metabolism
the enzyme is part of the 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation cycle, pahway overview
metabolism
the enzyme is part of the proposed reductive pathway for 3-hydroxypropionate assimilation by Rhodobacter sphaeroides 2.4.1, overview
metabolism
-
the enzyme is part of the 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation cycle, pahway overview
-
metabolism
-
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
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
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
two-hybrid assay analysis of the protein interaction of ACR and SSR in Saccharomyces cerevisiae
additional information
-
two-hybrid assay analysis of the protein interaction of ACR and SSR in Saccharomyces cerevisiae
additional information
-
two-hybrid assay analysis of the protein interaction of ACR and SSR in Saccharomyces cerevisiae
-