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
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autotrophic
- metallosphaera
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3-hydroxypropionate/4-hydroxybutyrate
- sedula
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malonyl-coenzyme
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acetyl-coenzyme
- succinyl-coa
- propionyl-coa
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acrylic
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value-added
- synthesis
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transhydrogenase
- sulfolobales
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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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Substrates Products
Substrates Products on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)
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REACTION DIAGRAM
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
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r
malonate semialdehyde + NADPH + H+
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spectrophotometric product determination
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r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
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?
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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malonate-semialdehyde + NADPH + H+
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3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, additionally exhibits 3-hydroxypropionate dehydrogenase activity
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3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
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r
3-hydroxypropanoate + NAD+
NADH can partially substitute (20% activity) for NADPH
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?
malonate semialdehyde + NADH + H+
3-hydroxypropanoate + NAD+
NADH can partially substitute (20% activity) for NADPH
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3-hydroxypropanoate + NADP+
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malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
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?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
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?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
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?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
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?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
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malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
NADH can partially substitute (20% activity) for NADPH
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?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
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malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
NADH can partially substitute (20% activity) for NADPH
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3-hydroxypropionate + NADP+
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malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
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MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
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additional information
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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
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additional information
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enzyme is part of an autotrophic CO2 fixation pathway in which acetyl-CoA is carboxylated and reductively converted via 3-hydroxypropionate to propionyl-CoA. Propionyl-CoA is carboxylated and converted via succinyl-CoA and CoA transfer to malyl-CoA. Malyl-CoA is cleaved to acetyl-CoA and glyoxylate. Thereby, the first CO, acceptor molecule acetyl-CoA is regenerated, completing the cycle and the net CO, fixation product glyoxylate is released
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additional information
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bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
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additional information
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the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
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additional information
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the bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75. The C-terminal subdomain MCR-C reduces malonyl-CoA to malonate semialdehyde, while the N-terminal subdomain MCR-N reduces malonate semialdehyde to 3-HP
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additional information
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the bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75. The C-terminal subdomain MCR-C reduces malonyl-CoA to malonate semialdehyde, while the N-terminal subdomain MCR-N reduces malonate semialdehyde to 3-HP
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additional information
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the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
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additional information
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the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview
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additional information
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the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview
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additional information
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the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview
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additional information
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succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
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additional information
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succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
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additional information
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succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
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