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EC Number
Natural Substrates
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Reversibility
shikimate dehydrogenase
more
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
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shikimate dehydrogenase
more
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
?
-
?
shikimate dehydrogenase
more
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
?
-
?
shikimate dehydrogenase
more
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
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ketol-acid reductoisomerase (NADP+)
more
the enzyme is involved in biosynthesis of branched chain amino acids valine, isoleucine, and leucine, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
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tropinone reductase I
tropinone + NADPH + H+
reaction of tropinone reductase I, EC 1.1.1.206, tropane alkaloid biosynthesis, overview
tropine + NADP+
leading to formation of tropane alkaloids
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quinate/shikimate dehydrogenase
more
the enzyme preferentially uses quinate as a substrate in vitro like a quinate dehydrogenase, EC 1.1.1.24, with only residual shikimate dehydrogenase, SDH, activity, cf. EC 1.1.1.25
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3-hydroxypropionate dehydrogenase (NADP+)
more
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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3-hydroxypropionate dehydrogenase (NADP+)
more
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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L-lactate dehydrogenase (cytochrome)
(S)-lactate + 2 ferricytochrome c
replaces activity of EC 1.1.1.27 in limited substrate conditions
pyruvate + 2 ferrocytochrome c + 2 H+
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Results 1 - 10 of 12 > >>