1.2.1.19: aminobutyraldehyde dehydrogenase

This is an abbreviated version!
For detailed information about aminobutyraldehyde dehydrogenase, go to the full flat file.

Reaction

Synonyms

4-aminobutanal dehydrogenase, 4-aminobutyraldehyde dehydrogenase, ABAL dehydrogenase, ABALDH, ALDH10A8, ALDH10A9, AMADH, AMADH1, AMADH2, aminoaldehyde dehydrogenase, BADH, betaine aldehyde dehydrogenase, dehydrogenase, aminobutyraldehyde, EC 1.5.1.35, gadbh, gamma-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydroganase, gamma-aminobutyraldehyde dehydrogenase, gamma-guanidinobutyraldehyde dehydrogenase, MdAMADH1, MdAMADH2, More, NAD+-aminoaldehyde dehydrogenase, NAD+-dependent aminoaldehyde dehydrogenase, PatD, PsAMADH 1, PsAMADH 2, SlAMADH1, SlAMADH2, YdcW, ZmAMADH1a, ZmAMADH1b, ZmAMADH2

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.19 aminobutyraldehyde dehydrogenase

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2	Activating Compound
3602	AA Sequence
2	Application
1	CAS Registry Number
17	Cloned(Commentary)
42	Cofactor
4	Crystallization (Commentary)
25	Disease/ Diagnostics
7	Expression
22	General Information
3	General Stability
36	Inhibitors
37	kcat/KM [mM/s]
7	Ki Value [mM]
150	KM Value [mM]
19	Localization
4	Metals/Ions
19	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
63	Organism
12	Pathway
62	PDB ID
26	pH Optimum
10	pH Range
1	pH Stability
2	pI Value
4	Protein Variants
19	Purification (Commentary)
2	Reaction
3	Reaction Type
49	Reference
41	Source Tissue
38	Specific Activity [micromol/min/mg]
5	Storage Stability
199	Substrates and Products (Substrate)
18	Subunits
83	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
1	Temperature Range [°C]
23	Temperature Stability [°C]
69	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

isozyme AMADH1 in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 13% (w/v) PEG 6000 and 5% (v/v) 2-methyl-2,4-pentanediol, at 20°C

Pisum sativum

Q8VWZ1, Q93YB2

712753

isozyme AMADH2 in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 18% (w/v) PEG 4000, 10% (v/v) isopropanol and 0.5% (w/v) n-octyl beta-D-glucopyranoside, at 20°C

Pisum sativum

Q8VWZ1, Q93YB2

712753

wild-type SlAMADH1 with 5 mM NAD+is crystallized over a reservoir containing 23% PEG 1000, 0.1 M HEPES, pH 7.5, mutant E260A of SlAMADH1 with 5 mM NAD+ is crystallized over a reservoir containing 15% PEG 1500, 0.1 M imidazole, pH 7.0, and 10% glycerol, sitting drop vapor diffusion method, cryoprotectant solution consits of mother liquor supplemented with 25% PEG 400 for SlAMADH1 or 20% glycerol for the E260A mutant, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model

Solanum lycopersicum

B6ECN9

742854

wild-type ZnAMADH1a with 5 mM NAD+ is crystallized over a reservoir containing 16% PEG 4000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, sitting drop vapor diffusion method, cryoprotection by 20% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model

Zea mays

C0P9J6, C6KEM4, G5DDC2

742854