4.2.1.127: linalool dehydratase

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For detailed information about linalool dehydratase, go to the full flat file.

Reaction

Synonyms

bifunctional linalool dehydratase isomerase, LDI, ldi/LDI, linalool dehydratase isomerase, linalool dehydratase-isomerase, linalool dehydratase/isomerase, LinD, LIS, More

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.1 Hydro-lyases

                4.2.1.127 linalool dehydratase

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Results	in table
6	Activating Compound
14	AA Sequence
4	Application
4	Cloned(Commentary)
2	Cofactor
3	Crystallization (Commentary)
2	Expression
24	General Information
13	Inhibitors
2	KM Value [mM]
6	Localization
1	Metals/Ions
3	Molecular Weight [Da]
20	Natural Substrates/ Products (Substrates)
46	Organism
3	Pathway
35	PDB ID
5	pH Optimum
1	pH Range
2	Posttranslational Modification
10	Protein Variants
4	Purification (Commentary)
7	Reaction
16	Reference
2	Source Tissue
2	Specific Activity [micromol/min/mg]
46	Substrates and Products (Substrate)
11	Subunits
39	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Range [°C]

Crystallization

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Crystallization on EC 4.2.1.127 - linalool dehydratase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

analysis of enzyme structure from crystal structure of the enzyme complexed with (S)-linalool, PDB ID 5G1U

Castellaniella defragrans

E1XUJ2

748867

purified recombinant enzyme Ldi, free or in complex with thiomersal and/or linalool, sitting and hanging drop vapor diffusion method, 4 different crystallization methods, using PEG 550 MME, DTT, and bicine buffer, pH 9.0, overview. X-ray diffraction structure determination and analysis at 1.9 A resolution, single isomorphous replacement anomalous scattering method using thimerosal as heavy metal compound

Castellaniella defragrans

E1XUJ2

747771

purified wild-type enzyme LinD alone or in complex with geraniol, or as selenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 1.76-2.68 A resolution

Castellaniella defragrans

E1XUJ2

748734