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
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autoinduction
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phosphopantetheinylation
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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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Reaction
Reaction on EC 1.2.1.30 - carboxylate reductase (NADP+)
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing diphosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O-atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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