1.2.1.30: carboxylate reductase (NADP+)
This is an abbreviated version!
For detailed information about carboxylate reductase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.30
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1.2.1.30
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synthesis
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bio-based
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fragrance
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autoinduction
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phosphopantetheinylation
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over-reduction
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benzaldehyde
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industry
- 1.2.1.30
- synthesis
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bio-based
-
fragrance
-
autoinduction
-
phosphopantetheinylation
-
over-reduction
- benzaldehyde
- industry
Reaction
Synonyms
aromatic acid reductase, aryl aldehyde:NADP+ oxidoreductase, aryl-aldehyde dehydrogenase (NADP+), aryl-aldehyde oxidoreductase, ATP/NADPH-dependent carboxylic acid reductase, CAR, carboxylate reductase, carboxylate reductases, Carboxylic acid reductase, kaCAR, mab3CAR, maCAR, mmCAR, mpCAR, msCAR, naCAR, NcCAR, niCAR, noCAR, tpCAR, type I CAR, type III CAR
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Posttranslational Modification
Posttranslational Modification on EC 1.2.1.30 - carboxylate reductase (NADP+)
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phosphopantetheinylation
side-chain modification
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posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
-
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
-
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
-
phosphopantetheinylation
-
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
-
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
-
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
phosphopantetheinylation
-
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
side-chain modification
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The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
side-chain modification
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
side-chain modification
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
side-chain modification
-
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-