1.2.1.10: acetaldehyde dehydrogenase (acetylating)

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For detailed information about acetaldehyde dehydrogenase (acetylating), go to the full flat file.

Reaction

Synonyms

4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, ACDH, acetaldehyde dehydrogenase, Acetaldehyde dehydrogenase [acetylating], acetaldehyde-alcohol dehydrogenase, acetyl-CoA reductase, acylating acetaldehyde dehydrogenase, AdhE, ADHES77, aldehyde dehydrogenase, aldehyde dehydrogenase (acylating), aldehyde/alcohol dehydrogenase, ALDH, BAD, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, BphJ, CoA-acylating aldehyde dehydrogenase, CoA-dependent aldehyde dehydrogenase, coenzyme A linked aldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, DmpF, DmpFG, MhpF, More, NAD+/CoA-dependent aldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, PduP, Teth514_0627, Teth514_1942, Tsac_0416, TTHB247

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.10 acetaldehyde dehydrogenase (acetylating)

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Results	in table
8	Activating Compound
8247	AA Sequence
9	Application
1	CAS Registry Number
18	Cloned(Commentary)
69	Cofactor
3	Crystallization (Commentary)
3	Expression
21	General Information
7	General Stability
25	Inhibitors
39	kcat/KM [mM/s]
4	Ki Value [mM]
94	KM Value [mM]
13	Localization
3	Metals/Ions
33	Molecular Weight [Da]
40	Natural Substrates/ Products (Substrates)
256	Organism
1	Oxidation Stability
31	Pathway
36	PDB ID
17	pH Optimum
10	pH Range
2	pH Stability
1	pI Value
16	Protein Variants
19	Purification (Commentary)
8	Reaction
4	Reaction Type
55	Reference
3	Source Tissue
31	Specific Activity [micromol/min/mg]
10	Storage Stability
151	Substrates and Products (Substrate)
29	Subunits
65	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
4	Temperature Range [°C]
8	Temperature Stability [°C]
26	Turnover Number [1/s]

Expression

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Expression on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

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

2 entries

expression is strongly influenced by the pH of the culture medium. Expression in cells grown on ethanol is higher at pH 6.0 than at pH 3.7

Polytomella sp. Pringsheim 198.80

Q70YJ9

739328

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

Chlamydomonas reinhardtii

Q1RS84

763253

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

Chlamydomonas reinhardtii CC-124

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