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
ECTree
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Activating Compound
Activating Compound on EC 1.2.1.30 - carboxylate reductase (NADP+)
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dithiothreitol
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stimulation of the reduction of the intermediate benzoyladenosine 5'-monophosphate to benzaldehyde
phosphopantetheine transferase
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required for activating the enzyme. Recombinant car is an apoenzyme that requires phosphopantetheinylation for conversion to a fully active holoenzyme
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for activation, CARs require PPTase-mediated post-translational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
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additional information
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for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
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additional information
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
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additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
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additional information
levels of recombinant Car and Gdh are slightly higher when cultures are grown without chloramphenicol
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additional information
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated post-translational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
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