1.1.1.298: 3-hydroxypropionate dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about 3-hydroxypropionate dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.1.1.298
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1.1.1.298
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acetyl-coa
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aurantiacus
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carboxylase
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chloroflexus
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autotrophic
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metallosphaera
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3-hydroxypropionate/4-hydroxybutyrate
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sedula
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malonyl-coenzyme
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acetyl-coenzyme
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succinyl-coa
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propionyl-coa
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acrylic
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value-added
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synthesis
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transhydrogenase
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sulfolobales
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reductase-dependent
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crenarchaeota
- 1.1.1.298
- acetyl-coa
- aurantiacus
- carboxylase
- chloroflexus
-
autotrophic
- metallosphaera
-
3-hydroxypropionate/4-hydroxybutyrate
- sedula
-
malonyl-coenzyme
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acetyl-coenzyme
- succinyl-coa
- propionyl-coa
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acrylic
-
value-added
- synthesis
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transhydrogenase
- sulfolobales
-
reductase-dependent
- crenarchaeota
Reaction
Synonyms
3-HIBADH, 3-hydroxyisobutyrate dehydrogenase, 3-hydroxypropionate dehydrogenase, bi-functional malonyl-CoA reductase, malonate semialdehyde reductase, malonate semialdehyde reductase (NADPH), malonic semialdehyde reductase, malonyl-CoA reductase, MCR, More, MSAR, Msed_1993
ECTree
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General Information
General Information on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)
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evolution
metabolism
physiological function
additional information
distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview
evolution
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distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview
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the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
metabolism
3-hydroxypropionic acid (3HP) production via MCR dependent pathway, overview. The bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75
metabolism
enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview
metabolism
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from acetate via malonyl-CoA in the malonyl-CoA reductase pathway, enzyme MCR shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview
metabolism
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from malonyl-CoA via the malonyl-CoA reductase pathway, it shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview
metabolism
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from malonyl-CoA via the malonyl-CoA reductase pathway, it shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid. 3HP can be produced from several intermediates, such as glycerol, malonyl-CoA, and beta-alanine. Among all these biosynthetic routes, the malonyl-CoA pathway has some distinct advantages, including a broad feedstock spectrum, thermodynamic feasibility, and redox neutrality. Comparison of the different metabolic routes for 3HP biosynthesis from glycerol or glucose, overview
metabolism
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the enzyme from Escherichia coli synthesizes 3-hydroxypropionate (3-HP) from malonate semialdehyde via the beta-alanine pathway, overview. The transformation of beta-alanine to malonic semialdehyde relies on GABT (gamma-aminobutyrate transaminase) and BAPAT (beta-alanine-pyruvate aminotransferase)
metabolism
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the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
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metabolism
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enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview
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enzyme is part of an autotrophic 3-hydroxypropionate/4-hydroxybutyrate carbon dioxide assimilation pathway in Metallospaera sedula. In the pathway, CO2 is fixed with acetyl-CoA/propionyl-CoA carboxylase as key carboxylating enzyme. One acetyl-CoA and two bicarbonate molecules are reductively converted via 3-hydroxypropionate to succinyl-CoA
physiological function
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the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
physiological function
the organism assimilates CO2 by the 3-hydroxypropionate cycle, and malonyl-CoA reductase is an essential enzyme for the cycle
physiological function
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from malonyl-CoA via the malonyl-CoA reductase pathway, it shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview
physiological function
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the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
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physiological function
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the organism assimilates CO2 by the 3-hydroxypropionate cycle, and malonyl-CoA reductase is an essential enzyme for the cycle
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Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR)
additional information
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Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR)
additional information
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Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR)
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