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Literature summary extracted from

  • Van Lis, R.; Popek, M.; Coute, Y.; Kosta, A.; Drapier, D.; Nitschke, W.; Atteia, A.
    Concerted up-regulation of aldehyde/alcohol dehydrogenase (ADHE) and starch in Chlamydomonas reinhardtii increases survival under dark anoxia (2017), J. Biol. Chem., 292, 2395-2410 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.1 gene adhE, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis Chlamydomonas reinhardtii
1.2.1.10 gene adhE, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis Chlamydomonas reinhardtii

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.1 additional information generation of enzyme overexpressing mutant strain 10-6C, which is a photosynthetic mutant impaired in CO2 assimilation because of a point mutation in the RBCL gene Chlamydomonas reinhardtii
1.2.1.10 additional information generation of enzyme overexpressing mutant strain 10-6C, which is a photosynthetic mutant impaired in CO2 assimilation because of a point mutation in the RBCL gene Chlamydomonas reinhardtii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 additional information
-
 additional information Michaelis-Menten kinetics Chlamydomonas reinhardtii
1.2.1.10 additional information
-
 additional information Michaelis-Menten kinetics Chlamydomonas reinhardtii
1.2.1.10 0.0127
-
 acetyl-CoA pH 7.0, temperature not specified in the publication Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.1 chloroplast stroma
-
 Chlamydomonas reinhardtii 9570
-
1.1.1.1 additional information the enzyme protein exhibits an extended N-terminus (about 60 residues), which serves as an intracellular targeting signal Chlamydomonas reinhardtii
-
-
1.2.1.10 chloroplast stroma
-
 Chlamydomonas reinhardtii 9570
-
1.2.1.10 additional information the enzyme protein exhibits an extended N-terminus (about 60 residues), which serves as an intracellular targeting signal Chlamydomonas reinhardtii
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 Fe2+ the residues potentially involved in iron coordination are Asp727, His731, His797, and His811. Two signatures for iron-binding are identified in the ADH domain: ADH_iron_1 (residues 706-734) and ADH_iron_2 (residues 794-814) Chlamydomonas reinhardtii
1.2.1.10 Fe2+ the residues potentially involved in iron coordination are Asp727, His731, His797, and His811. Two signatures for iron-binding are identified in the ADH domain: ADH_iron_1 (residues 706-734) and ADH_iron_2 (residues 794-814) Chlamydomonas reinhardtii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.1 180000 440000 dimeric-tetrameric enzyme, native PAGE Chlamydomonas reinhardtii
1.2.1.10 180000 440000 dimeric-tetrameric enzyme, native PAGE Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.1 acetaldehyde + NADH + H+ Chlamydomonas reinhardtii
-
 ethanol + NAD+
-
 r
1.1.1.1 acetaldehyde + NADH + H+ Chlamydomonas reinhardtii CC-124
-
 ethanol + NAD+
-
 r
1.1.1.1 additional information Chlamydomonas reinhardtii the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate ?
-
-
1.1.1.1 additional information Chlamydomonas reinhardtii CC-124 the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate ?
-
-
1.2.1.10 acetyl-CoA + NADH + H+ Chlamydomonas reinhardtii
-
 acetaldehyde + CoA + NAD+
-
 r
1.2.1.10 additional information Chlamydomonas reinhardtii the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate ?
-
-
1.2.1.10 additional information Chlamydomonas reinhardtii CC-124 the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Chlamydomonas reinhardtii Q1RS84
-
-
1.1.1.1 Chlamydomonas reinhardtii CC-124 Q1RS84
-
-
1.2.1.10 Chlamydomonas reinhardtii Q1RS84
-
-
1.2.1.10 Chlamydomonas reinhardtii CC-124 Q1RS84
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.1 native enzyme from chloroplast stroma by anion exchange chromatography and affinity chromatography, followed by ultracentrifugation Chlamydomonas reinhardtii
1.2.1.10 native enzyme from chloroplast stroma by anion exchange chromatography and affinity chromatography, followed by ultracentrifugation Chlamydomonas reinhardtii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 acetaldehyde + NADH + H+
-
 Chlamydomonas reinhardtii ethanol + NAD+
-
 r
1.1.1.1 acetaldehyde + NADH + H+
-
 Chlamydomonas reinhardtii CC-124 ethanol + NAD+
-
 r
1.1.1.1 additional information the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate Chlamydomonas reinhardtii ?
-
-
1.1.1.1 additional information ADHE catalyzes the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde Chlamydomonas reinhardtii ?
-
-
1.1.1.1 additional information the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate Chlamydomonas reinhardtii CC-124 ?
-
-
1.1.1.1 additional information ADHE catalyzes the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde Chlamydomonas reinhardtii CC-124 ?
-
-
1.2.1.10 acetyl-CoA + NADH + H+
-
 Chlamydomonas reinhardtii acetaldehyde + CoA + NAD+
-
 r
1.2.1.10 additional information the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate Chlamydomonas reinhardtii ?
-
-
1.2.1.10 additional information ADHE catalyzes the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde Chlamydomonas reinhardtii ?
-
-
1.2.1.10 additional information the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate Chlamydomonas reinhardtii CC-124 ?
-
-
1.2.1.10 additional information ADHE catalyzes the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde Chlamydomonas reinhardtii CC-124 ?
-
-

Subunits

EC Number Subunits Comment Organism
1.1.1.1 homodimer 2* 80000, SDS-PAGE Chlamydomonas reinhardtii
1.1.1.1 homotetramer 4 * 80000, SDS-PAGE Chlamydomonas reinhardtii
1.1.1.1 More the enzyme is associated in dimers and higher order oligomers in the chloroplast. Domain structure, overview. In contrast to the native enzyme, the recombinant ADHE associates most predominantly into dimers. The native enzyme mostly occurs in multiple oligomeric forms Chlamydomonas reinhardtii
1.2.1.10 homodimer 2 * 80000, SDS-PAGE Chlamydomonas reinhardtii
1.2.1.10 homotetramer 4 * 80000, SDS-PAGE Chlamydomonas reinhardtii
1.2.1.10 More the enzyme is associated in dimers and higher order oligomers in the chloroplast. Domain structure, overview. In contrast to the native enzyme, the recombinant ADHE associates most predominantly into dimers. The native enzyme mostly occurs in multiple oligomeric forms Chlamydomonas reinhardtii

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 AdhE
-
 Chlamydomonas reinhardtii
1.1.1.1 aldehyde/alcohol dehydrogenase
-
 Chlamydomonas reinhardtii
1.1.1.1 More see also EC 1.2.1.10 Chlamydomonas reinhardtii
1.2.1.10 AdhE
-
 Chlamydomonas reinhardtii
1.2.1.10 aldehyde/alcohol dehydrogenase
-
 Chlamydomonas reinhardtii
1.2.1.10 More see also EC 1.1.1.1 Chlamydomonas reinhardtii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 6.5 7 assay at Chlamydomonas reinhardtii
1.2.1.10 6.5 7 assay at Chlamydomonas reinhardtii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+
-
 Chlamydomonas reinhardtii
1.1.1.1 NADH NADH binding sites are Gly270-Gly291 and Glu599-Met622 Chlamydomonas reinhardtii
1.2.1.10 acetyl-CoA
-
 Chlamydomonas reinhardtii
1.2.1.10 CoA
-
 Chlamydomonas reinhardtii
1.2.1.10 NAD+
-
 Chlamydomonas reinhardtii
1.2.1.10 NADH NADH binding sites are Gly270-Gly291 and Glu599-Met622 Chlamydomonas reinhardtii

Expression

EC Number Organism Comment Expression
1.1.1.1 Chlamydomonas reinhardtii ADHE is upregulated under oxic conditions. Upregulation is observed in cells exposed to diverse physiological stresses, including zinc deficiency, nitrogen starvation, and inhibition of carbon concentration/fixation capacity. Cells with increased ADHE abundance exhibit better survival under dark anoxia. Zinc deficiency increases ADHE accumulation and fermentative abilities. Lack of RubisCO carboxylase activity or carbonic anhydrase 3, and impaired starch synthesis also induce the enzyme up
1.2.1.10 Chlamydomonas reinhardtii ADHE is upregulated under oxic conditions. Upregulation is observed in cells exposed to diverse physiological stresses, including zinc deficiency, nitrogen starvation, and inhibition of carbon concentration/fixation capacity. Cells with increased ADHE abundance exhibit better survival under dark anoxia. Zinc deficiency increases ADHE accumulation and fermentative abilities. Lack of RubisCO carboxylase activity or carbonic anhydrase 3, and impaired starch synthesis also induce the enzyme up

General Information

EC Number General Information Comment Organism
1.1.1.1 evolution distribution of ADHE among the five eukaryotic supergroups, overview Chlamydomonas reinhardtii
1.1.1.1 malfunction cells with increased ADHE abundance exhibit better survival under dark anoxia Chlamydomonas reinhardtii
1.1.1.1 metabolism analysis of the anerobic metabolic routes involving the enzyme in Chlamydomonas reinhardtii, overview Chlamydomonas reinhardtii
1.1.1.1 physiological function aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes Chlamydomonas reinhardtii
1.2.1.10 evolution distribution of ADHE among the five eukaryotic supergroups, overview Chlamydomonas reinhardtii
1.2.1.10 malfunction cells with increased ADHE abundance exhibit better survival under dark anoxia Chlamydomonas reinhardtii
1.2.1.10 metabolism analysis of the anerobic metabolic routes involving the enzyme in Chlamydomonas reinhardtii, overview Chlamydomonas reinhardtii
1.2.1.10 physiological function aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes Chlamydomonas reinhardtii