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Literature summary for 1.2.1.30 extracted from
- Carboxylic acid reductases in etabolic engineering (2020), J. Biotechnol., 307, 1-14 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | for activation, CARs require PPTase-mediated post-translational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Aspergillus niger | |
| additional information | for activation, CARs require PPTase-mediated post-translational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Trametes versicolor | |
| additional information | for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Neurospora crassa | |
| additional information | for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Moorella thermoacetica | |
| additional information | for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Nocardia asteroides | |
| additional information | for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Nocardia iowensis | |
| additional information | for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Mycobacteroides abscessus | |
| additional information | for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites | Mycobacterium marinum |
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Neurospora crassa |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Aspergillus niger |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Moorella thermoacetica |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Nocardia asteroides |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Trametes versicolor |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Recombinant enzyme expression in Saccharomyces cerevisiae and Saccharomyces pombe and an engineered aldehyde-accumulating Escherichia coli strain for de novo production of vanillin from glucose. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Nocardia iowensis |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. The CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18, expanding the potential of CARs in synthetic pathways. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Mycobacteroides abscessus |
| synthesis | carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. The CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18, expanding the potential of CARs in synthetic pathways. Aldehydes as reactive intermediates in biosynthetic pathways, overview | Mycobacterium marinum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli resulting in decreased activity due to a lack of post-translational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity. Coexpression with the recombinant phosphopantetheinyl transferase (PPTase) from Bacillus subtilis (Sfp) or cell-free extracts from Nocardia iowensis containing native PPTase converted niCAR to its holoenzyme state, increases the enzyme activity 20fold. Recombinant enzyme expression in Saccharomyces cerevisiae and Saccharomyces pombe and an engineered aldehyde-accumulating Escherichia coli strain for de novo production of vanillin from glucose | Nocardia iowensis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Neurospora crassa |  |
| Mg2+ | required | Aspergillus niger | |
| Mg2+ | required | Moorella thermoacetica | |
| Mg2+ | required | Nocardia asteroides | |
| Mg2+ | required | Trametes versicolor | |
| Mg2+ | required | Nocardia iowensis | |
| Mg2+ | required | Mycobacteroides abscessus | |
| Mg2+ | required | Mycobacterium marinum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| benzoate + NADPH + H+ + ATP | Nocardia asteroides | - |
benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| benzoate + NADPH + H+ + ATP | Neurospora crassa | via an adenylated intermediate | benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| benzoate + NADPH + H+ + ATP | Nocardia iowensis | via an adenylated intermediate | benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
| Moorella thermoacetica | - |
- |
- |
| Mycobacterium marinum | B2HN69 | - |
- |
| Mycobacterium marinum ATCC BAA-535 | B2HN69 | - |
- |
| Mycobacteroides abscessus | - |
- |
- |
| Neurospora crassa | - |
- |
- |
| Nocardia asteroides | - |
- |
- |
| Nocardia iowensis | Q6RKB1 | - |
- |
| Trametes versicolor | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Neurospora crassa |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Aspergillus niger |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Moorella thermoacetica |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Nocardia asteroides |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Trametes versicolor |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Nocardia iowensis |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Mycobacteroides abscessus |
| phosphopantetheinylation | posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity | Mycobacterium marinum |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | Aspergillus niger | |
| 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 | Neurospora crassa | |
| 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 | Moorella thermoacetica | |
| 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 | Nocardia asteroides | |
| 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 | Trametes versicolor | |
| 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 | Nocardia iowensis | |
| 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 | Mycobacteroides abscessus | |
| 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 | Mycobacterium marinum |
Substrates and Products (Substrate)
| 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 | - |
Aspergillus niger | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Moorella thermoacetica | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Nocardia asteroides | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Trametes versicolor | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Nocardia iowensis | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Mycobacteroides abscessus | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Mycobacterium marinum | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| aromatic carboxylate + NADPH + H+ + ATP | - |
Mycobacterium marinum ATCC BAA-535 | aromatic aldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| benzoate + NADPH + H+ + ATP | - |
Nocardia asteroides | benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| benzoate + NADPH + H+ + ATP | via an adenylated intermediate | Neurospora crassa | benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| benzoate + NADPH + H+ + ATP | via an adenylated intermediate | Nocardia asteroides | benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| benzoate + NADPH + H+ + ATP | via an adenylated intermediate | Nocardia iowensis | benzaldehyde + NADP+ + AMP + diphosphate | - |
ir | |
| additional information | 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 | Neurospora crassa | ? | - |
- |
|
| additional information | 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 | Aspergillus niger | ? | - |
- |
|
| additional information | 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 | Moorella thermoacetica | ? | - |
- |
|
| additional information | 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 | Nocardia asteroides | ? | - |
- |
|
| additional information | 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 | Trametes versicolor | ? | - |
- |
|
| additional information | 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 | Nocardia iowensis | ? | - |
- |
|
| additional information | 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 | Mycobacteroides abscessus | ? | - |
- |
|
| additional information | 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 | Mycobacterium marinum | ? | - |
- |
|
| additional information | 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 | Mycobacterium marinum ATCC BAA-535 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Neurospora crassa |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Aspergillus niger |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Moorella thermoacetica |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Nocardia asteroides |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Trametes versicolor |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Nocardia iowensis |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Mycobacteroides abscessus |
| More | the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study | Mycobacterium marinum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aryl-aldehyde oxidoreductase | - |
Neurospora crassa |
| aryl-aldehyde oxidoreductase | - |
Aspergillus niger |
| aryl-aldehyde oxidoreductase | - |
Moorella thermoacetica |
| aryl-aldehyde oxidoreductase | - |
Nocardia asteroides |
| aryl-aldehyde oxidoreductase | - |
Trametes versicolor |
| aryl-aldehyde oxidoreductase | - |
Nocardia iowensis |
| aryl-aldehyde oxidoreductase | - |
Mycobacteroides abscessus |
| aryl-aldehyde oxidoreductase | - |
Mycobacterium marinum |
| CAR | - |
Neurospora crassa |
| CAR | - |
Aspergillus niger |
| CAR | - |
Moorella thermoacetica |
| CAR | - |
Nocardia asteroides |
| CAR | - |
Trametes versicolor |
| CAR | - |
Nocardia iowensis |
| CAR | - |
Mycobacteroides abscessus |
| CAR | - |
Mycobacterium marinum |
| Carboxylic acid reductase | - |
Neurospora crassa |
| Carboxylic acid reductase | - |
Aspergillus niger |
| Carboxylic acid reductase | - |
Moorella thermoacetica |
| Carboxylic acid reductase | - |
Nocardia asteroides |
| Carboxylic acid reductase | - |
Trametes versicolor |
| Carboxylic acid reductase | - |
Nocardia iowensis |
| Carboxylic acid reductase | - |
Mycobacteroides abscessus |
| Carboxylic acid reductase | - |
Mycobacterium marinum |
| mab3CAR | - |
Mycobacteroides abscessus |
| mmCAR | - |
Mycobacterium marinum |
| naCAR | - |
Nocardia asteroides |
| NcCAR | - |
Neurospora crassa |
| niCAR | - |
Nocardia iowensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Neurospora crassa | |
| ATP | - |
Aspergillus niger | |
| ATP | - |
Moorella thermoacetica | |
| ATP | - |
Nocardia asteroides | |
| ATP | - |
Trametes versicolor | |
| ATP | - |
Nocardia iowensis | |
| ATP | - |
Mycobacteroides abscessus | |
| ATP | - |
Mycobacterium marinum | |
| NADPH | - |
Neurospora crassa | |
| NADPH | - |
Aspergillus niger | |
| NADPH | - |
Moorella thermoacetica | |
| NADPH | - |
Nocardia asteroides | |
| NADPH | - |
Trametes versicolor | |
| NADPH | - |
Nocardia iowensis | |
| NADPH | - |
Mycobacteroides abscessus | |
| NADPH | - |
Mycobacterium marinum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | CAR phylogenetic analysis and tree | Neurospora crassa |
| evolution | CAR phylogenetic analysis and tree | Aspergillus niger |
| evolution | CAR phylogenetic analysis and tree | Moorella thermoacetica |
| evolution | CAR phylogenetic analysis and tree | Nocardia asteroides |
| evolution | CAR phylogenetic analysis and tree | Trametes versicolor |
| evolution | CAR phylogenetic analysis and tree | Nocardia iowensis |
| evolution | CAR phylogenetic analysis and tree | Mycobacteroides abscessus |
| evolution | CAR phylogenetic analysis and tree | Mycobacterium marinum |
| malfunction | lack of posttranslational phosphopantetheinylation of a serine group in the recombinant CAR reduces the activity of recombinantly expressed enzyme | Nocardia iowensis |
| 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 | Mycobacteroides abscessus |
| additional information | structure-function analysis and structure comparisons | Neurospora crassa |
| additional information | structure-function analysis and structure comparisons | Aspergillus niger |
| additional information | structure-function analysis and structure comparisons | Moorella thermoacetica |
| additional information | structure-function analysis and structure comparisons | Nocardia asteroides |
| additional information | structure-function analysis and structure comparisons | Trametes versicolor |
| additional information | structure-function analysis and structure comparisons | Nocardia iowensis |
| additional information | structure-function analysis and structure comparisons | Mycobacteroides abscessus |
| additional information | structure-function analysis and structure comparisons | Mycobacterium marinum |
| 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 | Neurospora crassa |
| 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 | Aspergillus niger |
| 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 | Moorella thermoacetica |
| 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 | Nocardia asteroides |
| 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 | Mycobacteroides abscessus |
| 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 | Mycobacterium marinum |
| 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) | Nocardia iowensis |
| 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 | Trametes versicolor |
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Release 2023.1 (January 2023)
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