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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
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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
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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
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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
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
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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
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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
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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
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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
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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
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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
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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
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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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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
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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
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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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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
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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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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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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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
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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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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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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(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
2-methoxybenzoate + NADPH + H+ + ATP
2-methoxybenzaldehyde + NADP+ + AMP + diphosphate
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Substrates: -
Products: -
?
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
3-hydroxypropionate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
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Substrates: -
Products: -
ir
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
4-hydroxybutyrate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
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Substrates: -
Products: -
ir
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
4-nitrobenzoate + NADPH + H+ + ATP
4-nitrobenzaldehyde + NADP+ + AMP + diphosphate
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Substrates: -
Products: -
?
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
5-hydroxypentanoate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
alpha-ketoglutaric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
benzaldehyde + NADP+ + benzoyladenosine 5'-monophosphate + phosphate
benzoate + NADPH + ATP
-
Substrates: -
Products: -
r
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
benzoic acid + ATP + NADPH + H+
benzaldehyde + AMP + diphosphate + NADP+
Substrates: highest turnover number
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + benzyl alcohol + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
butyric acid + ATP + NADPH + H+
butyraldehyde + AMP + diphosphate + NADP+
Substrates: -
Products: highest Km value
?
caffeic acid + NADPH + ATP
3-(3,4-dihydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
capric acid + ATP + NADPH + H+
capraldehyde + AMP + diphosphate + NADP+
Substrates: -
Products: -
?
caproic acid + ATP + NADPH + H+
caproaldehyde + AMP + diphosphate + NADP+
Substrates: -
Products: -
?
caprylic acid + ATP + NADPH + H+
caprylaldehyde + AMP + diphosphate + NADP+
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
cis-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
citric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
coniferic acid + NADPH + ATP
coniferyl aldehyde + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
D-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
DL-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
fatty acid + ATP + NADPH + H+
fatty aldehyde + AMP + diphosphate + NADP+
Substrates: -
Products: -
?
ferulic acid + NADPH + H+ + ATP
3-(4-hydroxy-3-methoxyphenyl)-2-propen-1-al + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
ferulic acid + NADPH + H+ + ATP
ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + diphosphate
Substrates: not completely reduced
Products: -
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
glutarate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
L-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
lauric acid + ATP + NADPH + H+
lauraldehyde + AMP + diphosphate + NADP+
Substrates: highest catalytic efficiency
Products: -
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
malonate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
sinapic acid + NADPH + ATP
3-(4-hydroxy-3,5-dimethoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
succinate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
trans-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
Substrates: -
Products: -
?
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
vanillic acid + NADPH + H+ + ATP
vanillin + vanillyl alcohol + NADP+ + AMP + diphosphate
-
Substrates: with Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant Npt is expressed along with recombinant car, vanillic acid is reduced to vanillin and vanillyl alcohol, with vanillin (80%) as the major product. Escherichia coli BL21-CodonPlus(DE3)-RP/pHAT305 (expressing only recombinant Car) reduce only 50% of the vanillic acid starting material, with vanillyl alcohol being the major metabolite. With Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant car is presumed to be in the fully active, phosphopantetheinylated holo form, the rate of reduction of vanillic acid is much faster than that of vanillin to vanillyl alcohol by endogenous Escherichia coli aldehyde dehydrogenase
Products: -
?
additional information
?
-
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
Nocadia sp.
-
Substrates: -
Products: -
?
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
Substrates: -
Products: -
?
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
r
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp.
-
Substrates: -
Products: -
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp. NRRL 5646
-
Substrates: -
Products: -
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
Substrates: -
Products: -
?
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
-
Substrates: -
Products: -
?
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
Substrates: best substrate
Products: -
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: via an adenylated intermediate
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: via an adenylated intermediate
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Substrates: via an adenylated intermediate
Products: -
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: rate relative to salycilate 286%
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Nocadia sp.
-
Substrates: the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Nocadia sp. NRRL 5646
-
Substrates: the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
Nocadia sp.
-
Substrates: -
Products: -
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
Substrates: -
Products: -
?
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
Substrates: low activity
Products: -
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
Substrates: low activity
Products: -
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
Substrates: low activity
Products: -
ir
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
Substrates: -
Products: -
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
Substrates: rate relative to benzoate 9%
Products: -
?
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
Substrates: -
Products: -
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
ir
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
-
Substrates: no activity of the wild-type enzyme with succinate. Substrate specificity of recombinant hybrid mutant enzymes, overview
Products: -
-
additional information
?
-
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
-
Substrates: substrate specificity of recombinant hybrid mutant enzymes, overview
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
Substrates: substrate specificity of recombinant hybrid mutant enzymes, overview
Products: -
-
additional information
?
-
Substrates: the enzyme is active against C2-C18 fatty acids. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
Products: -
-
additional information
?
-
Substrates: the enzyme is active against C2-C18 fatty acids. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: substrate specificity of recombinant hybrid mutant enzymes, overview
Products: -
-
additional information
?
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
-
Substrates: no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, phenylpropynoate, butanoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
Products: -
-
additional information
?
-
-
Substrates: enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity. No activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, phenylpropynoate, pyridine-2-carboxylate, and 1H-pyrrole-2-carboxylate
Products: -
-
additional information
?
-
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
Substrates: NcCAR wild-type and mutants efficiently reduce aliphatic acids
Products: -
-
additional information
?
-
-
Substrates: substrate specificity of recombinant hybrid mutant enzymes, overview
Products: -
-
additional information
?
-
Substrates: NcCAR wild-type and mutants efficiently reduce aliphatic acids
Products: -
-
additional information
?
-
Substrates: NcCAR wild-type and mutants efficiently reduce aliphatic acids
Products: -
-
additional information
?
-
Substrates: NcCAR wild-type and mutants efficiently reduce aliphatic acids
Products: -
-
additional information
?
-
Substrates: NcCAR wild-type and mutants efficiently reduce aliphatic acids
Products: -
-
additional information
?
-
Substrates: NcCAR wild-type and mutants efficiently reduce aliphatic acids
Products: -
-
additional information
?
-
Nocadia sp.
-
Substrates: other substrates are phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, polyaromatic ring carboxylic acids, ibuprofen and its (R)-(-) isomer
Products: -
?
additional information
?
-
Nocadia sp. NRRL 5646
-
Substrates: other substrates are phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, polyaromatic ring carboxylic acids, ibuprofen and its (R)-(-) isomer
Products: -
?
additional information
?
-
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
-
Substrates: the enzyme prefers benzoates and aliphatic acids that are substituted with a phenyl group in the 3-position. No reaction of this CAR with simple aliphatic acids
Products: -
-
additional information
?
-
-
Substrates: the enzyme prefers benzoates and aliphatic acids that are substituted with a phenyl group in the 3-position. No reaction of this CAR with simple aliphatic acids
Products: -
-
additional information
?
-
-
Substrates: enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
Products: -
-
additional information
?
-
Substrates: pyruvic, isocitric acid, fumaric acid and maleic acid are not substrates for the enzyme
Products: -
?
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
Substrates: no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
Products: -
-
additional information
?
-
-
Substrates: substrate specificity of recombinant hybrid mutant enzymes, overview
Products: -
-
additional information
?
-
-
Substrates: no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, 1H-pyrrole-2-carboxylate and furan-2-carboxylate
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
Substrates: CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
Products: -
-
additional information
?
-
-
Substrates: the enzyme is active against C2-C18 fatty acids
Products: -
-
additional information
?
-
-
Substrates: carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
Products: -
-
additional information
?
-
-
Substrates: the enzyme is active against C2-C18 fatty acids
Products: -
-
additional information
?
-
-
Substrates: no activity with 2-nitrobenzoate and 1H-pyrrole-2-carboxylate
Products: -
-
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evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
analysis of highly conserved signature sequences of CARs, overview
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
CAR phylogenetic analysis and tree
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
CAR phylogenetic analysis and tree
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
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evolution
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analysis of highly conserved signature sequences of CARs, overview
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evolution
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analysis of highly conserved signature sequences of CARs, overview
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evolution
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analysis of highly conserved signature sequences of CARs, overview
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evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
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evolution
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analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
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malfunction
lack of posttranslational phosphopantetheinylation of a serine group in the recombinant CAR reduces the activity of recombinantly expressed enzyme
malfunction
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
malfunction
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the purified CAR with a mutation to its conserved serine idue appears to degrade into separate A- and R-domains when incubated at room temperature
malfunction
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replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
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malfunction
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replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
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malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
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malfunction
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replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
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physiological function
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carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
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carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
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CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Enzyme CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. The purified enzyme from Nocardia iowensis reduces a broader range of substituted aromatic acids in addition to dicarboxylic acids of the citric acid cycle, resulting in a branding of the aryl-aldehyde oxidoreductase class more broadly as carboxylic acid reductases (CARs)
physiological function
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CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Whole cell reduction of aromatic carboxylic acids in the white-rot fungi Trametes versicolor
physiological function
requirement for the presence of a phosphopantetheine transferase for the loading of a phosphopantetheine group onto the CAR enzyme is shown for niCAR. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
physiological function
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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
physiological function
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
physiological function
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
physiological function
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
physiological function
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
physiological function
-
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
-
physiological function
-
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
-
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
-
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Enzyme CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18
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physiological function
-
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
-
physiological function
-
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
-
physiological function
-
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
-
physiological function
-
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
-
physiological function
-
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
-
physiological function
-
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
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additional information
structure homology modeling
additional information
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analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synt