1.2.1.75: malonyl-CoA reductase (malonate semialdehyde-forming)
This is an abbreviated version!
For detailed information about malonyl-CoA reductase (malonate semialdehyde-forming), go to the full flat file.
Reaction
Synonyms
bi-functional malonyl-CoA reductase, malonate semialdehyde reductase, malonate-semialdehyde dehydrogenase, malonyl CoA reductase (malonate semialdehyde-forming), malonyl-CoA reductase, MCR, More, MSAR
ECTree
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Substrates Products
Substrates Products on EC 1.2.1.75 - malonyl-CoA reductase (malonate semialdehyde-forming)
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REACTION DIAGRAM
malonate semialdehyde + coenzyme A + NADP+
malonyl-CoA + NADPH + H+
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r
malonyl-CoA + NADPH + H+
malonate semialdehyde + NADP+ + CoA
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-
-
-
?
succinate semialdehyde + coenzyme A + NADP+
succinyl-CoA + NADPH + H+
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-
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r
succinyl-CoA + NADPH + H+
succinate semialdehyde + coenzyme A + NADP+
at 25% of the rate with malonyl-CoA
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r
3-hydroxypropionic acid + NADP+
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?
malonate semialdehyde + NADPH + H+
3-hydroxypropionic acid + NADP+
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?
malonate semialdehyde + CoA + NADP+
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism
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?
malonate semialdehyde + coenzyme A + NADP+
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + coenzyme A + NADP+
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r
succinic semialdehyde + CoA + NADP+
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?
succinyl-CoA + NADPH + H+
succinic semialdehyde + CoA + NADP+
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?
?
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enzyme additionally catalyzes the second reduction step of malonate semialdehyde + NADPH + H+ to 3-hydroxypropionate + NADP+. Reverse reaction starting with 3-hydroxypropionate does not require CoA and probably stops at malonate semialdehyde. No substrates are acetyl-CoA, propionyl-CoA, succinyl-CoA, or glyoxylate
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?
additional information
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the bifunctional enzyme shows malonate semialdehyde reduction activity, EC 1.1.1.298, and also malonyl-CoA reduction activity. 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 malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, and the reduction of malonate semialdehyde to 3-hydroxypropionate, cf. EC 1.1.1.298, 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, and the reduction of malonate semialdehyde to 3-hydroxypropionate, cf. EC 1.1.1.298, 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, and the reduction of malonate semialdehyde to 3-hydroxypropionate, cf. EC 1.1.1.298, 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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