1.2.1.30	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	-, 763290	
1.2.1.30	evolution	analysis of highly conserved signature sequences of CARs, overview	-, 763083	
1.2.1.30	evolution	CAR phylogenetic analysis and tree	-, 763297	
1.2.1.30	malfunction	lack of posttranslational phosphopantetheinylation of a serine group in the recombinant CAR reduces the activity of recombinantly expressed enzyme	763297	
1.2.1.30	malfunction	replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity	-, 763083	
1.2.1.30	malfunction	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	763297	
1.2.1.30	additional information	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	-, 763290	
1.2.1.30	additional information	structure homology modeling	-, 763083	
1.2.1.30	additional information	structure-function analysis and structure comparisons	-, 763297	
1.2.1.30	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	-, 763295	
1.2.1.30	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	763297	
1.2.1.30	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	-, 763297	
1.2.1.30	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)	763297	
1.2.1.30	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. Whole cell reduction of aromatic carboxylic acids in the white-rot fungi Trametes versicolor	763297	
1.2.1.30	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	762919	
1.2.1.30	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	-, 763290