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Literature summary extracted from

  • Kramer, L.; Le, X.; Hankore, E.D.; Wilson, M.A.; Guo, J.; Niu, W.
    Engineering and characterization of hybrid carboxylic acid reductases (2019), J. Biotechnol., 304, 52-56 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.30 E697Q site-directed mutagenesis, the mutant enzyme retains 48.8% of wild-type activity with benzoate substrate Mycobacterium avium
1.2.1.30 additional information hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from fungus Neurospora crassa (Nc), resulting in hybrid enzymes: Mav(A)-Nc(PR), Mav(AP)-Nc(R), Nc(A)-Mav(PR), and Nc(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes Neurospora crassa
1.2.1.30 additional information hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Kutzneria albida (Ka) resulting in hybrid enzymes: Mav(A)-Ka(PR), Mav(AP)-Ka(R), Ka(A)-Mav(PR), and Ka(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes Kutzneria albida
1.2.1.30 additional information hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm) resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), and Mm(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes Mycobacterium marinum
1.2.1.30 additional information hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm), Kutzneria albida (Ka), and Nocardia iowensis (Ni), and one fungal strain, Neurospora crassa (Nc), resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), Mm(AP)-Mav(R), Mav(A)-Ka(PR), Mav(AP)-Ka(R), Ka(A)-Mav(PR), Ka(AP)-Mav(R), Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs, overview. When mutations Q637E and E697Q are introduced into hybrid CAR, Mm(A)-Mav(PR), reduction in activities is also observed, albeit to a less extent. Analysis of substrate specificity of recombinant hybrid mutant enzymes Mycobacterium avium
1.2.1.30 additional information hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Nocardia iowensis (Ni) resulting in hybrid enzymes: Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes Nocardia iowensis
1.2.1.30 Q637E site-directed mutagenesis, the mutant enzyme retains 47.1% of wild-type activity with benzoate substrate Mycobacterium avium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.30 additional information
-
 additional information stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview Neurospora crassa
1.2.1.30 additional information
-
 additional information stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview Mycobacterium avium
1.2.1.30 additional information
-
 additional information stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview Kutzneria albida
1.2.1.30 additional information
-
 additional information stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview Nocardia iowensis
1.2.1.30 additional information
-
 additional information stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview Mycobacterium marinum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.30 Mg2+ required Neurospora crassa
1.2.1.30 Mg2+ required Mycobacterium avium
1.2.1.30 Mg2+ required Kutzneria albida
1.2.1.30 Mg2+ required Nocardia iowensis
1.2.1.30 Mg2+ required Mycobacterium marinum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.30 benzoate + NADPH + H+ + ATP Neurospora crassa
-
 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP Mycobacterium avium
-
 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP Kutzneria albida
-
 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP Nocardia iowensis
-
 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP Mycobacterium marinum
-
 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP Mycobacterium marinum ATCC BAA-535
-
 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP Neurospora crassa
-
 vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP Mycobacterium avium
-
 vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP Kutzneria albida
-
 vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP Nocardia iowensis
-
 vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP Mycobacterium marinum
-
 vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP Mycobacterium marinum ATCC BAA-535
-
 vanillin + NADP+ + AMP + diphosphate
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.30 Kutzneria albida
-
-
-
1.2.1.30 Mycobacterium avium
-
-
-
1.2.1.30 Mycobacterium marinum B2HN69
-
-
1.2.1.30 Mycobacterium marinum ATCC BAA-535 B2HN69
-
-
1.2.1.30 Neurospora crassa
-
-
-
1.2.1.30 Nocardia iowensis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.30 3-hydroxypropionate + NADPH + H+ + ATP
-
 Kutzneria albida 3-hydroxypropanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 3-hydroxypropionate + NADPH + H+ + ATP
-
 Nocardia iowensis 3-hydroxypropanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 3-hydroxypropionate + NADPH + H+ + ATP
-
 Mycobacterium marinum 3-hydroxypropanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 3-hydroxypropionate + NADPH + H+ + ATP
-
 Mycobacterium marinum ATCC BAA-535 3-hydroxypropanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 3-hydroxypropionate + NADPH + H+ + ATP
-
 Mycobacterium avium ? + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 4-hydroxybutyrate + NADPH + H+ + ATP
-
 Kutzneria albida 4-hydroxybutanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 4-hydroxybutyrate + NADPH + H+ + ATP
-
 Nocardia iowensis 4-hydroxybutanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 4-hydroxybutyrate + NADPH + H+ + ATP
-
 Mycobacterium marinum 4-hydroxybutanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 4-hydroxybutyrate + NADPH + H+ + ATP
-
 Mycobacterium marinum ATCC BAA-535 4-hydroxybutanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 4-hydroxybutyrate + NADPH + H+ + ATP
-
 Mycobacterium avium ? + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 5-hydroxypentanoate + NADPH + H+ + ATP
-
 Kutzneria albida 5-hydroxypentanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 5-hydroxypentanoate + NADPH + H+ + ATP
-
 Nocardia iowensis 5-hydroxypentanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 5-hydroxypentanoate + NADPH + H+ + ATP
-
 Mycobacterium marinum 5-hydroxypentanal + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 5-hydroxypentanoate + NADPH + H+ + ATP
-
 Mycobacterium avium ? + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP
-
 Neurospora crassa benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP
-
 Mycobacterium avium benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP
-
 Kutzneria albida benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP
-
 Nocardia iowensis benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP
-
 Mycobacterium marinum benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 benzoate + NADPH + H+ + ATP
-
 Mycobacterium marinum ATCC BAA-535 benzaldehyde + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 glutarate + NADPH + H+ + ATP
-
 Kutzneria albida 5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 glutarate + NADPH + H+ + ATP
-
 Nocardia iowensis 5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 glutarate + NADPH + H+ + ATP
-
 Mycobacterium marinum 5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 glutarate + NADPH + H+ + ATP
-
 Mycobacterium avium ? + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 malonate + NADPH + H+ + ATP low activity Kutzneria albida 3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 malonate + NADPH + H+ + ATP low activity Nocardia iowensis 3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 malonate + NADPH + H+ + ATP low activity Mycobacterium marinum 3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 malonate + NADPH + H+ + ATP
-
 Mycobacterium avium ? + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 additional information no activity of the wild-type enzyme with succinate. Substrate specificity of recombinant hybrid mutant enzymes, overview Kutzneria albida ?
-
-
1.2.1.30 additional information substrate specificity of recombinant hybrid mutant enzymes, overview Neurospora crassa ?
-
-
1.2.1.30 additional information substrate specificity of recombinant hybrid mutant enzymes, overview Mycobacterium avium ?
-
-
1.2.1.30 additional information substrate specificity of recombinant hybrid mutant enzymes, overview Nocardia iowensis ?
-
-
1.2.1.30 additional information substrate specificity of recombinant hybrid mutant enzymes, overview Mycobacterium marinum ?
-
-
1.2.1.30 additional information substrate specificity of recombinant hybrid mutant enzymes, overview Mycobacterium marinum ATCC BAA-535 ?
-
-
1.2.1.30 succinate + NADPH + H+ + ATP
-
 Nocardia iowensis 4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 succinate + NADPH + H+ + ATP
-
 Mycobacterium marinum 4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 succinate + NADPH + H+ + ATP
-
 Mycobacterium avium ? + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP
-
 Neurospora crassa vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP
-
 Mycobacterium avium vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP
-
 Kutzneria albida vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP
-
 Nocardia iowensis vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP
-
 Mycobacterium marinum vanillin + NADP+ + AMP + diphosphate
-
 ir
1.2.1.30 vanillate + NADPH + H+ + ATP
-
 Mycobacterium marinum ATCC BAA-535 vanillin + NADP+ + AMP + diphosphate
-
 ir

Synonyms

EC Number Synonyms Comment Organism
1.2.1.30 CAR
-
 Neurospora crassa
1.2.1.30 CAR
-
 Mycobacterium avium
1.2.1.30 CAR
-
 Kutzneria albida
1.2.1.30 CAR
-
 Nocardia iowensis
1.2.1.30 CAR
-
 Mycobacterium marinum
1.2.1.30 Carboxylic acid reductase
-
 Neurospora crassa
1.2.1.30 Carboxylic acid reductase
-
 Mycobacterium avium
1.2.1.30 Carboxylic acid reductase
-
 Kutzneria albida
1.2.1.30 Carboxylic acid reductase
-
 Nocardia iowensis
1.2.1.30 Carboxylic acid reductase
-
 Mycobacterium marinum
1.2.1.30 kaCAR
-
 Kutzneria albida
1.2.1.30 maCAR
-
 Mycobacterium marinum
1.2.1.30 mmCAR
-
 Mycobacterium avium
1.2.1.30 NcCAR
-
 Neurospora crassa
1.2.1.30 niCAR
-
 Nocardia iowensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.30 ATP
-
 Neurospora crassa
1.2.1.30 ATP
-
 Mycobacterium avium
1.2.1.30 ATP
-
 Kutzneria albida
1.2.1.30 ATP
-
 Nocardia iowensis
1.2.1.30 ATP
-
 Mycobacterium marinum
1.2.1.30 NADPH
-
 Neurospora crassa
1.2.1.30 NADPH
-
 Mycobacterium avium
1.2.1.30 NADPH
-
 Kutzneria albida
1.2.1.30 NADPH
-
 Nocardia iowensis
1.2.1.30 NADPH
-
 Mycobacterium marinum

General Information

EC Number General Information Comment Organism
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 Neurospora crassa
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 Mycobacterium avium
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 Kutzneria albida
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 Nocardia iowensis
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 Mycobacterium marinum