EC Number |
General Information |
Reference |
---|
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 | evolution |
analysis of highly conserved signature sequences of CARs, overview |
-, 763083 |
1.2.1.30 | malfunction |
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity |
-, 763083 |
1.2.1.30 | more |
structure homology modeling |
-, 763083 |
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 | more |
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 | 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 |
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 | 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 |