1.2.1.26: 2,5-dioxovalerate dehydrogenase

This is an abbreviated version!
For detailed information about 2,5-dioxovalerate dehydrogenase, go to the full flat file.

Reaction

Synonyms

2-oxoglutarate semialdehyde dehydrogenase, AbKGSADH, aldehyde dehydrogenase, ALDH, alpha-ketoglutarate semialdehyde dehydrogenase, alpha-ketoglutarate-semialdehyde dehydrogenase, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-KGSA dehydrogenase, alphaKGSA dehydrogenase, alphaKGSADH, araE, DopDH, KGSADH, KGSADH-I, KGSADH-II, KGSADH-III, More, SSO3117, ycbD protein

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.26 2,5-dioxovalerate dehydrogenase

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Results	in table
5	Activating Compound
933	AA Sequence
5	Application
1	CAS Registry Number
8	Cloned(Commentary)
16	Cofactor
1	Crystallization (Commentary)
5	General Information
3	Inhibitors
21	kcat/KM [mM/s]
56	KM Value [mM]
1	Metals/Ions
9	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
26	Organism
16	Pathway
4	PDB ID
6	pH Optimum
2	pH Range
18	Protein Variants
9	Purification (Commentary)
1	Reaction
3	Reaction Type
18	Reference
2	Source Tissue
1	Specific Activity [micromol/min/mg]
1	Storage Stability
55	Substrates and Products (Substrate)
11	Subunits
49	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
2	Temperature Stability [°C]
54	Turnover Number [1/s]

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General Information on EC 1.2.1.26 - 2,5-dioxovalerate dehydrogenase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

Azospirillum brasilense

Q1JUP4

low ALDH activity has been reported to cause intracellular accumulation of highly toxic 3-hydroxypropionaldehyde (3-HPA) seriously hampering the cell growth

763717

metabolism

Azospirillum brasilense

Q1JUP4

3-hydroxypropionate biosynthesis pathway from glycerol involves enzymes coenzyme B12-dependent glycerol dehydratase (DhaB) and aldehyde dehydrogenase (ALDH), overview. alpa-Ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH) can catalyze the ALDH reaction forming 3-hydroxypropionate

763717

physiological function

Azospirillum brasilense

Q1JUP4

alpa-ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH) can catalyze the ALDH reaction forming 3-hydroxypropionate, but it is not its physiological substrate

763717

additional information

3 entries

additional information

Azospirillum brasilense

Q1JUP4

molecular docking simulations of AbKGSADH with 2-oxoglutaric semialdehyde (alpha-KGSA) and succinate semialdehyde (SSA). Molecular docking simulations reveal that these two substrates fit well into the somewhat positively charged substrate binding pocket. The aldehyde-groups of these substrates, which are the sites of enzyme reaction, are located in the same place around the catalytic residues. The aldehyde-group of alpha-KGSA is stabilized by Gln160 and Arg163 through hydrogen bonds, and two catalytic residues, Glu253 and Cys287, also assist the binding of the molecule. The 4'-oxo-group of alpha-KGSA is stabilized by hydrogen bonds with Arg281, and the carboxyl-group of the molecule is stabilized by Glu106 and Gln160. The substrate binding pocket is also formed by several hydrophobic residues, such as Phe156, Val286, Ile288, Pro444, and Phe450, which seem to contribute to the stabilization of the hydrophobic part of alpha-KGSA. The binding of SSA is similar to that of alpha-KGSA, however, the stabilization of the carboxyl-group of SSA is quite different. Arg281, a residue that is involved in the stabilization of the 4'-oxo-group of alpha-KGSA, forms a hydrogen bond with the carboxyl-group of SSA instead. These observations explain how AbKGSADH can accommodate both alpha-KGSA and SSA as real substrates

763717

additional information

Azospirillum brasilense

-

molecular docking simulations of AbKGSADH with 2-oxoglutaric semialdehyde (alpha-KGSA) and succinate semialdehyde (SSA). Molecular docking simulations reveal that these two substrates fit well into the somewhat positively charged substrate binding pocket. The aldehyde-groups of these substrates, which are the sites of enzyme reaction, are located in the same place around the catalytic residues. The aldehyde-group of alpha-KGSA is stabilized by Gln160 and Arg163 through hydrogen bonds, and two catalytic residues, Glu253 and Cys287, also assist the binding of the molecule. The 4'-oxo-group of alpha-KGSA is stabilized by hydrogen bonds with Arg281, and the carboxyl-group of the molecule is stabilized by Glu106 and Gln160. The substrate binding pocket is also formed by several hydrophobic residues, such as Phe156, Val286, Ile288, Pro444, and Phe450, which seem to contribute to the stabilization of the hydrophobic part of alpha-KGSA. The binding of SSA is similar to that of alpha-KGSA, however, the stabilization of the carboxyl-group of SSA is quite different. Arg281, a residue that is involved in the stabilization of the 4'-oxo-group of alpha-KGSA, forms a hydrogen bond with the carboxyl-group of SSA instead. These observations explain how AbKGSADH can accommodate both alpha-KGSA and SSA as real substrates

763717

additional information

Azospirillum brasilense

Q1JUP4

residues E253 and C287 are predicted as the catalytic residues

763713