1.3.8.1: short-chain acyl-CoA dehydrogenase

This is an abbreviated version!
For detailed information about short-chain acyl-CoA dehydrogenase, go to the full flat file.

Reaction

Synonyms

3-hydroxyacyl CoA reductase, ACADS, Acfer_0556, Acfer_1477, acyl-CoA dehydrogenase short chain, BCAD, BCD, bcd2, BcdAf, bSCAD, butyryl CoA dehydrogenase, butyryl coenzyme A dehydrogenase, butyryl-CoA dehydrogenase, butyryl-CoA dehydrogenase complex, butyryl-CoA dehydrogenase/Etf complex, CD1054, dehydrogenase, butyryl coenzyme A, EC 1.3.2.1, EC 1.3.99.2, enoyl-coenzyme A reductase, ethylene reductase, HADHSC, non-dissociating bifurcating Etf-Bcd complex, SCAD, ScdA, short chain acyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-CoA dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, short-chain acylCoA dehydrogenase, unsaturated acyl coenzyme A reductase

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.8 With a flavin as acceptor

                1.3.8.1 short-chain acyl-CoA dehydrogenase

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Results	in table
3	Activating Compound
7829	AA Sequence
11	Application
1	CAS Registry Number
25	Cloned(Commentary)
30	Cofactor
3	Crystallization (Commentary)
692	Disease/ Diagnostics
2	Expression
22	General Information
2	General Stability
37	Inhibitors
6	kcat/KM [mM/s]
4	Ki Value [mM]
78	KM Value [mM]
23	Localization
3	Metals/Ions
33	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
145	Organism
2	Oxidation Stability
19	Pathway
39	PDB ID
17	pH Optimum
9	pH Range
5	pH Stability
2	pI Value
2	Posttranslational Modification
47	Protein Variants
27	Purification (Commentary)
6	Reaction
3	Reaction Type
102	Reference
1	Renatured (Commentary)
48	Source Tissue
39	Specific Activity [micromol/min/mg]
10	Storage Stability
178	Substrates and Products (Substrate)
19	Subunits
83	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Temperature Stability [°C]
42	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.3.8.1 - short-chain acyl-CoA dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified enzyme, mixing of 15 mg/ml protein solution with 225% PEG 1500, 10% SPG buffer, pH 9.0, at 4°C, X-ray diffraction structure determination and analysis at 1.8 A resolution

Acidaminococcus fermentans

D2RIQ3, D2RIQ3; D2RL84

742866

hanging- or sitting-drop method, 120 mM potassium phosphate, pH 6.0, 60 mM Bis-Tris acetate, pH 6.0, 190 mM ammonium sulfate, 4.3% poly(ethylene glycol) 4500, resolution 2.5 A, space group P422, monomer consists of three domains: 2 alpha-helical domains at the N- and C-terminal regions and a beta-sheet in the middle, FAD is located between the beta-domain and the C-terminal domain of one subunit and the C-terminal domain of a neighboring subunit

Megasphaera elsdenii

-

391305

crystals of SCAD complexed with acetoacetyl-CoA are grown by sitting drop vapor diffusion, 8.8 mg/ml SCAD in the presence of 1.2 molar equivalents of acetoacetyl-CoA in 85 mM Tris-acetate, pH 7.0 and 270 mM amonium sulfate are equilibrated against a solution containing 85 mM Tris-acetate, pH 7.0 and 3.78 M ammonium sulfate, crystals diffract to 2.25 A

Rattus norvegicus

P15651

656039