Literature summary for 4.8.1.2 extracted from

Sawai, H.; Sugimoto, H.; Kato, Y.; Asano, Y.; Shiro, Y.; Aono, S.
X-ray crystal structure of michaelis complex of aldoxime dehydratase (2009), J. Biol. Chem., 284, 32089-32096.

Application

Application	Comment	Organism
biotechnology	nitrile compounds are important intermediates in some industrial processes to produce nylon and acrylic fibers, insecticides, and pharmaceuticals. A more environmentally benign process of aldoxime dehydration is needed, for which a biological dehydration of aldoxime is a possible candidate	Rhodococcus erythropolis

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rhodococcus erythropolis

Crystallization (Commentary)

Crystallization (Comment)	Organism
18% (w/v) PEG 4000, 0.075 M sodium cacodylate, 0.1 M magnesium acetate, pH 7.4, vapor diffusion, hanging drop, temperature 293 K, crystal structure of substrate-free form of aldoxime dehydratase, resolution 1.79 A, space group P1211, aldoxime dehydratase (OxdRE) in complex with propionaldoxime (soaked crystal), resolution 1.6 A, aldoxime dehydratase (OxdRE) in complex with butyraldoxime (co-crystal), resolution 2.5 A, aldoxime dehydratase (OxdRE) in complex with butyraldoxime (soaked crystal), resolution 1.8 A	Rhodococcus erythropolis

Crystallization (Comment)

Organism

18% (w/v) PEG 4000, 0.075 M sodium cacodylate, 0.1 M magnesium acetate, pH 7.4, vapor diffusion, hanging drop, temperature 293 K, crystal structure of substrate-free form of aldoxime dehydratase, resolution 1.79 A, space group P1211, aldoxime dehydratase (OxdRE) in complex with propionaldoxime (soaked crystal), resolution 1.6 A, aldoxime dehydratase (OxdRE) in complex with butyraldoxime (co-crystal), resolution 2.5 A, aldoxime dehydratase (OxdRE) in complex with butyraldoxime (soaked crystal), resolution 1.8 A

Rhodococcus erythropolis

Protein Variants

Protein Variants	Comment	Organism
E143Q	loss in enzymatic activity, 14% of the wild-type	Rhodococcus erythropolis
F306A	loss in enzymatic activity, 33% of the wild-type	Rhodococcus erythropolis
H320A	loss in enzymatic activity, 11% of the wild-type	Rhodococcus erythropolis
R178Q	loss in enzymatic activity, 36% of the wild-type	Rhodococcus erythropolis
S219A	loss in enzymatic activity, 23% of the wild-type	Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
alkylaldoxime	Rhodococcus erythropolis	-	alkylnitrile + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Rhodococcus erythropolis	Q76K71	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Rhodococcus erythropolis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
(Z)-phenylacetaldoxime	-	Rhodococcus erythropolis	phenylacetonitrile + H2O	-	?
alkylaldoxime	-	Rhodococcus erythropolis	alkylnitrile + H2O	-	?
butyraldoxime	-	Rhodococcus erythropolis	butyronitrile + H2O	-	?
propionaldoxime	-	Rhodococcus erythropolis	propionitrile + H2O	-	?

Subunits

Subunits	Comment	Organism
homodimer	each monomer contains one heme molecule	Rhodococcus erythropolis

Synonyms

Synonyms	Comment	Organism
aldoxime dehydratase	-	Rhodococcus erythropolis
OXD	-	Rhodococcus erythropolis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
5.1	-	(Z)-phenylacetaldoxime	mutant enzyme H320A, pH 7.0, 30°C	Rhodococcus erythropolis
6.8	-	(Z)-phenylacetaldoxime	mutant enzyme E143Q, pH 7.0, 30°C	Rhodococcus erythropolis
11.1	-	(Z)-phenylacetaldoxime	mutant enzyme S219A, pH 7.0, 30°C	Rhodococcus erythropolis
15.7	-	(Z)-phenylacetaldoxime	mutant enzyme F306A, pH 7.0, 30°C	Rhodococcus erythropolis
17.2	-	(Z)-phenylacetaldoxime	mutant enzyme R178Q, pH 7.0, 30°C	Rhodococcus erythropolis
47.3	-	(Z)-phenylacetaldoxime	wild-type enzyme, pH 7.0, 30°C	Rhodococcus erythropolis

Cofactor

Cofactor	Comment	Organism	Structure
heme	each monomer contains one heme molecule	Rhodococcus erythropolis