1.2.1.47: 4-trimethylammoniobutyraldehyde dehydrogenase

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For detailed information about 4-trimethylammoniobutyraldehyde dehydrogenase, go to the full flat file.

Reaction

Synonyms

4-N-trimethylaminobutyraldehyde dehydrogenase, 4-N-trimethylaminobutyraldehyde dehydrogenase II, 4-trimethylaminobutyraldehyde dehydrogenase, 4-trimethylammoniobutyraldehyde dehydrogenase, aldehyde dehydrogenase 9A1, Aldh9a1, carnitine biosynthesis enzyme, dehydrogenase, trimethylaminobutyraldehyde, gamma-trimethylaminobutyraldehyde dehydrogenase, TMABA dehydrogenase, TMABA-DH, TMABADH, TMABAL dehydrogenase, TMABaldehyde-DH II, TMABALDH

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.47 4-trimethylammoniobutyraldehyde dehydrogenase

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Results	in table
1	Activating Compound
30	AA Sequence
1	Application
1	CAS Registry Number
5	Cloned(Commentary)
16	Cofactor
2	Crystallization (Commentary)
9	Disease/ Diagnostics
3	Expression
6	General Information
1	General Stability
44	Inhibitors
5	Ki Value [mM]
36	KM Value [mM]
8	Localization
1	Metals/Ions
9	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
19	Organism
5	Pathway
30	PDB ID
6	pH Optimum
1	pH Range
2	pH Stability
2	pI Value
7	Purification (Commentary)
1	Reaction
4	Reaction Type
18	Reference
54	Source Tissue
16	Specific Activity [micromol/min/mg]
3	Storage Stability
69	Substrates and Products (Substrate)
11	Subunits
36	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
3	Temperature Stability [°C]

Crystallization

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Crystallization on EC 1.2.1.47 - 4-trimethylammoniobutyraldehyde dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified human ALDH9A1 in apoform and in complex with NAD+ or 4-(trimethylamino)butyraldehyde, hanging drop vapour diffusion method, mixing of 28 mg/ml protein in 50 mM Tris/HCl, pH 7.5, and 150 mM NaCl, with 50 mM NAD+ and an equal volume of a precipitant solution containing 12% w/v PEG 4000, 0.1 M sodium citrate, pH 5.6, and 2.5% isopropanol, X-ray diffraction structure determination and analysis at 2.3 A, 2.9 A, and 2.5 A resolution, molecular replacement using the structure of BADH from Gadus morhua subsp. callarias liver as a search model (PDB IDs 1BPW and 1A4S), structure modeling

Homo sapiens

P49189

762831

purified recombinant detagged enzyme in complex with NAD+ and inhibitor diethylaminobenzaldehyde, hanging drop vapour diffusion method, mixing of 6 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 600 mM NaCl, 5% glycerol, 0.5 mM TCE, 5 mM DEAB, and 10 mM NAD+, with reservoir solution containing 0.1 M NaCl, 0.05 M Bis-Tris, pH 6.5, 0.1 M ammonium acetate, 0.05 M HEPES, pH 7.5, and 25% w/v PEG 3350, method optimization, X-ray diffraction structure determination and analysis at 2.50-2.64 A resolution, molecular replacement using structures of cod liver betaine ALDH (PDB ID 1A4S) and apo-ALDH9A1 (PDB ID 6QAP) as search models, modeling

Homo sapiens

P49189

762675