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Literature summary for 1.2.1.10 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)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii Q1RS84
-
-
Chlamydomonas reinhardtii CC-124 Q1RS84
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits Comment Organism
homodimer 2 * 80000, SDS-PAGE Chlamydomonas reinhardtii
homotetramer 4 * 80000, SDS-PAGE Chlamydomonas reinhardtii
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

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7 assay at Chlamydomonas reinhardtii

Cofactor

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

Expression

Organism Comment Expression
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

General Information Comment Organism
evolution distribution of ADHE among the five eukaryotic supergroups, overview Chlamydomonas reinhardtii
malfunction cells with increased ADHE abundance exhibit better survival under dark anoxia Chlamydomonas reinhardtii
metabolism analysis of the anerobic metabolic routes involving the enzyme in Chlamydomonas reinhardtii, overview Chlamydomonas reinhardtii
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