4.2.1.33: 3-isopropylmalate dehydratase

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For detailed information about 3-isopropylmalate dehydratase, go to the full flat file.

Reaction

Synonyms

3-isopropylmalate dehydratase, 3-isopropylmalate isomerase, Alpha-IPM isomerase, alpha-isopropylmalate isomerase, beta-Isopropylmalate dehydratase, dehydratase,beta-isopropylmalate, IPM dehydratase, IPM isomerase, IPMI, IPMI SSU1, isopropylmalate dehydratase, isopropylmalate isomerase, LEU1S, leuC, LeuCD, LeuD, MJ0499, More, SOI10, Superoxide-inducible protein 10

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.1 Hydro-lyases

                4.2.1.33 3-isopropylmalate dehydratase

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Results	in table
4	Activating Compound
81275	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
5	Crystallization (Commentary)
3	Expression
17	General Information
11	General Stability
39	Inhibitors
10	KM Value [mM]
7	Localization
6	Metals/Ions
9	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
223	Organism
5	Pathway
18	PDB ID
9	pH Optimum
5	pH Range
2	pH Stability
5	Protein Variants
7	Purification (Commentary)
8	Reaction
3	Reaction Type
30	Reference
11	Source Tissue
6	Specific Activity [micromol/min/mg]
1	Storage Stability
41	Substrates and Products (Substrate)
15	Subunits
62	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]

Crystallization

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Crystallization on EC 4.2.1.33 - 3-isopropylmalate dehydratase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol monomethyl ether 2000 and 0.1 MTris-HCl (pH 7.9)

Methanocaldococcus jannaschii

Q58673

729127

sitting-drop vapour-diffusion methodand hanging-drop vapour diffusion at 20°C, structures of oxidized and reduced forms of the large subunit of isopropylmalate isomerase (ox-MJ0499 and red-MJ0499, respectively) are reported at 1.8 and 2.7 A resolution, respectively. Significant large conformational changes are observed in the active site of red-MJ0499 when compared with ox-MJ0499

Methanocaldococcus jannaschii

P81291

726596

small subunit LeuD variants, X-ray diffraction structure determination and analysis at resolutions of 2.0 A for LeuD_1-156, 1.2 A for LeuD_1-168, and 2.5 A for LeuD_1-186, respectively

Mycobacterium tuberculosis

P9WK95, P9WQF5

716886

variants LeuD-1-156 and LeuD-1-168, by sitting-drop vapour-diffusion method, crystals of LeuD-1-156 belong to the hexagonal system (space group P6122 or P6522) with up to four subunits in the asymmetric unit, whereas the crystals of LeuD-1-168 belong to the monoclinic system (space group P21) with two subunits in the asymmetric unit. Both crystals diffract to beyond 2.0 A resolution

Mycobacterium tuberculosis

-

701510

crystal structure isopropylmalate isomerase small subunit. Four molecules create an interlocked assembly with intermolecular disulfide linkages having a skewed 222 point-group symmetry. The structure reveals the formation of intermolecular disulfide linkages, and it provides insight into the dual substrate specificity of the enzyme

Pyrococcus horikoshii

O59393

722946