EC Number   |
Reaction |
Reference |
|---|
   1.2.1.30 | an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP |
- |
- |
| 1.2.1.30 | 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 |
763297 |
| 1.2.1.30 | 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 |
-, 763297 |
| 1.2.1.30 | 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 |
-, 762919 |
| 1.2.1.30 | 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 |
762919 |
| 1.2.1.30 | 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 |
-, 763290 |
