4.1.3.4: hydroxymethylglutaryl-CoA lyase

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For detailed information about hydroxymethylglutaryl-CoA lyase, go to the full flat file.

Reaction

Synonyms

3-hydroxy-3-methylglutarate-CoA lyase, 3-Hydroxy-3-methylglutaryl CoA cleaving enzyme, 3-hydroxy-3-methylglutaryl CoA lyase, 3-Hydroxy-3-methylglutaryl coenzyme A lyase, 3-Hydroxy-3-methylglutaryl-CoA lyase, 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, 3-hydroxy-3-methylglutaryl-coenzyme A lyase, 3-hydroxy-methylglutaryl coenzyme A lyase, beta-hydroxy-beta-methylglutaryl-CoA lyase, HCL1, HL, HMG CoA cleavage enzyme, HMG CoA lyase, HMG-CoA lyase, HMGCL, HMGCLL1, HMGL, Hydroxymethylglutaryl coenzyme A lyase, Hydroxymethylglutaryl coenzyme A-cleaving enzyme, LiuE protein

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.3 Oxo-acid-lyases

                4.1.3.4 hydroxymethylglutaryl-CoA lyase

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Results	in table
7	Activating Compound
12314	AA Sequence
9	Application
1	CAS Registry Number
22	Cloned(Commentary)
7	Crystallization (Commentary)
602	Disease/ Diagnostics
7	General Information
2	General Stability
5	IC50 Value
24	Inhibitors
9	Ki Value [mM]
23	KM Value [mM]
30	Localization
34	Metals/Ions
18	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
50	Organism
1	Oxidation Stability
10	Pathway
30	PDB ID
13	pH Optimum
3	pH Range
2	pI Value
1	Posttranslational Modification
80	Protein Variants
21	Purification (Commentary)
6	Reaction
2	Reaction Type
50	Reference
44	Source Tissue
48	Specific Activity [micromol/min/mg]
6	Storage Stability
46	Substrates and Products (Substrate)
14	Subunits
60	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
1	Temperature Stability [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.1.3.4 - hydroxymethylglutaryl-CoA lyase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapour diffusion method with 22.5% (w/v) PEG 3350, 210 mM sodium iodide, 5 mM EDTA, 10 mM dithiothreitol

Bacillus subtilis

O34873

665744

hanging-drop vapour diffusion method

Bacillus subtilis

O34873

665744

hanging drop vapour diffusion method with 19% (w/v) PEG 3350, 200 mM CaCl2, 10 mM dithiothreitol

Brucella melitensis

Q8YEF2

665744

hanging-drop vapour diffusion method

Brucella melitensis

Q8YEF2

665744

crystal structure at 2.1 A resolution of the recombinant mitochondrial HMG-CoA lyase containing a bound activator cation and 3-hydroxyglutarate. For crystallization experiments, the enzyme is diluted to 5 –6 mg/ml. The competitive inhibitor hydroxyglutaryl-CoA is added to the diluted protein at about 1mM concentration. The inhibitor is necessary for generation of uniform diffraction quality crystals. Crystals sufficient for X-ray studies are obtained using an equilibration buffer of 0.1 M Hepes, pH 7.5, 60 mM MgCl2,and 15% polyethylene glycol 8K. The enzyme is mixed 1:1 with the equilibration buffer using sitting drop trays at 19°C. Crystals belong to the monoclinic space group C2 with unit cell parameters a = 197.0 A, b = 117.1 A, c = 86.8 A, and beta = 112.5°. Six monomers are found in the asymmetric unit

Homo sapiens

-

665743

sitting drop vapour diffusion method with 0.1 M HEPES, pH 7.5, 60 mM MgCl2, and 15% polyethylene glycol 8K

Homo sapiens

-

665743

vapor diffusion method

Homo sapiens

-

715529