Application | Comment | Organism |
---|---|---|
synthesis | the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level | Neurospora crassa |
synthesis | the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level | Nocardia iowensis |
synthesis | the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level | Mycobacterium marinum |
synthesis | the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level | Segniliparus rotundus |
synthesis | the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level | Aspergillus terreus |
Cloned (Comment) | Organism |
---|---|
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli | Nocardia iowensis |
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli | Mycobacterium marinum |
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli | Segniliparus rotundus |
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli | Aspergillus terreus |
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme with Escherichia coli phosphopantetheinyl transferase, EcPPTase, in Escherichia coli strain MG1655 RARE | Neurospora crassa |
Protein Variants | Comment | Organism |
---|---|---|
E337A | site-directed mutagenesis, mutant shows decreased activity compared to wild-type | Neurospora crassa |
E433A | site-directed mutagenesis, mutant shows decreased activity compared to wild-type | Neurospora crassa |
G432A | site-directed mutagenesis, the mutant shows activity similar to wild-type | Neurospora crassa |
H237A | site-directed mutagenesis, mutant shows decreased activity compared to wild-type | Neurospora crassa |
K190A | site-directed mutagenesis, the mutant shows increased activity compared to wild-type | Neurospora crassa |
K848A | site-directed mutagenesis, inactive mutant | Neurospora crassa |
additional information | analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively | Neurospora crassa |
additional information | analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively | Nocardia iowensis |
additional information | analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively | Mycobacterium marinum |
additional information | analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively | Segniliparus rotundus |
additional information | analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively | Aspergillus terreus |
P189A | site-directed mutagenesis, the mutant shows activity similar to wild-type | Neurospora crassa |
P234A | site-directed mutagenesis, the mutant shows increased activity compared to wild-type | Neurospora crassa |
T186A | site-directed mutagenesis, the mutant shows activity similar to wild-type | Neurospora crassa |
Y844A | site-directed mutagenesis, inactive mutant | Neurospora crassa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Neurospora crassa | |
Mg2+ | required | Nocardia iowensis | |
Mg2+ | required | Mycobacterium marinum | |
Mg2+ | required | Segniliparus rotundus | |
Mg2+ | required | Aspergillus terreus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
aromatic carboxylate + NADPH + H+ + ATP | Neurospora crassa | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Nocardia iowensis | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Mycobacterium marinum | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Segniliparus rotundus | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Aspergillus terreus | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Aspergillus terreus NIH 2624 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Mycobacterium marinum ATCC BAA-535 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Segniliparus rotundus CIP 108378 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Segniliparus rotundus ATCC BAA-972 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Segniliparus rotundus JCM 13578 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Aspergillus terreus FGSC A1156 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Segniliparus rotundus DSM 44985 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | Segniliparus rotundus CDC 1076 | - |
aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus terreus | Q0CRQ4 | - |
- |
Aspergillus terreus FGSC A1156 | Q0CRQ4 | - |
- |
Aspergillus terreus NIH 2624 | Q0CRQ4 | - |
- |
Mycobacterium marinum | B2HN69 | - |
- |
Mycobacterium marinum ATCC BAA-535 | B2HN69 | - |
- |
Neurospora crassa | - |
- |
- |
Nocardia iowensis | Q6RKB1 | - |
- |
Segniliparus rotundus | D6Z860 | - |
- |
Segniliparus rotundus ATCC BAA-972 | D6Z860 | - |
- |
Segniliparus rotundus CDC 1076 | D6Z860 | - |
- |
Segniliparus rotundus CIP 108378 | D6Z860 | - |
- |
Segniliparus rotundus DSM 44985 | D6Z860 | - |
- |
Segniliparus rotundus JCM 13578 | D6Z860 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
side-chain modification | 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 | Neurospora crassa |
side-chain modification | 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 | Nocardia iowensis |
side-chain modification | 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 | Mycobacterium marinum |
side-chain modification | 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 | Segniliparus rotundus |
side-chain modification | 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 | Aspergillus terreus |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration | Nocardia iowensis |
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration | Mycobacterium marinum |
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration | Segniliparus rotundus |
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration | Aspergillus terreus |
recombinant His-tagged enzyme from Escherichia coli strain MG1655 RARE by nickel affinity chromatography and desalting gel filtration | Neurospora crassa |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Neurospora crassa | |
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 | Nocardia iowensis | |
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 | Mycobacterium marinum | |
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 | Segniliparus rotundus | |
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 | Aspergillus terreus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
aromatic carboxylate + NADPH + H+ + ATP | - |
Neurospora crassa | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Nocardia iowensis | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Mycobacterium marinum | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Segniliparus rotundus | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Aspergillus terreus | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Aspergillus terreus NIH 2624 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Mycobacterium marinum ATCC BAA-535 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Segniliparus rotundus CIP 108378 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Segniliparus rotundus ATCC BAA-972 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Segniliparus rotundus JCM 13578 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Aspergillus terreus FGSC A1156 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Segniliparus rotundus DSM 44985 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
aromatic carboxylate + NADPH + H+ + ATP | - |
Segniliparus rotundus CDC 1076 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
cinnamate + NADPH + H+ + ATP | - |
Neurospora crassa | cinnamaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Neurospora crassa | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Nocardia iowensis | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Mycobacterium marinum | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Segniliparus rotundus | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Aspergillus terreus | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Aspergillus terreus NIH 2624 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Mycobacterium marinum ATCC BAA-535 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Segniliparus rotundus CIP 108378 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Segniliparus rotundus ATCC BAA-972 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Segniliparus rotundus JCM 13578 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Aspergillus terreus FGSC A1156 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Segniliparus rotundus DSM 44985 | ? | - |
- |
|
additional information | CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes | Segniliparus rotundus CDC 1076 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
More | the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine | Neurospora crassa |
More | the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine | Nocardia iowensis |
More | the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine | Mycobacterium marinum |
More | the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine | Segniliparus rotundus |
More | the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine | Aspergillus terreus |
Synonyms | Comment | Organism |
---|---|---|
CAR | - |
Neurospora crassa |
CAR | - |
Nocardia iowensis |
CAR | - |
Mycobacterium marinum |
CAR | - |
Segniliparus rotundus |
CAR | - |
Aspergillus terreus |
carboxylate reductase | - |
Neurospora crassa |
carboxylate reductase | - |
Nocardia iowensis |
carboxylate reductase | - |
Mycobacterium marinum |
carboxylate reductase | - |
Segniliparus rotundus |
carboxylate reductase | - |
Aspergillus terreus |
type I CAR | - |
Mycobacterium marinum |
type I CAR | - |
Segniliparus rotundus |
type III CAR | - |
Neurospora crassa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
28 | - |
assay at | Neurospora crassa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Neurospora crassa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Neurospora crassa | |
ATP | - |
Nocardia iowensis | |
ATP | - |
Mycobacterium marinum | |
ATP | - |
Segniliparus rotundus | |
ATP | - |
Aspergillus terreus | |
NADPH | - |
Neurospora crassa | |
NADPH | - |
Nocardia iowensis | |
NADPH | - |
Mycobacterium marinum | |
NADPH | - |
Segniliparus rotundus | |
NADPH | - |
Aspergillus terreus |
General Information | Comment | Organism |
---|---|---|
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 | Neurospora crassa |
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 | Nocardia iowensis |
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 | Mycobacterium marinum |
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 | Segniliparus rotundus |
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 | Aspergillus terreus |
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 | Neurospora crassa |
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 | Nocardia iowensis |
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 | Mycobacterium marinum |
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 | Segniliparus rotundus |
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 | Aspergillus terreus |
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 | Neurospora crassa |
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 | Nocardia iowensis |
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 | Mycobacterium marinum |
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 | Segniliparus rotundus |
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 | Aspergillus terreus |