Literature summary for 3.8.1.5 extracted from

Kennes, C.; Pries, F.; Krooshof, G.H.; Bokma, E.; Kingma, J.; Janssen, D.B.
Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity (1995), Eur. J. Biochem., 228, 403-407.

Search for more literature for 3.8.1.5

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
W125F	modified substrate binding properties	Escherichia coli
W125Q	modified substrate binding properties	Escherichia coli
W125R	modified substrate binding properties	Escherichia coli
W175Q	modified substrate binding properties	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
1-haloalkane + H2O = a primary alcohol + halide	catalytic mechanism	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
haloalkane + H2O	-	Escherichia coli	alcohol + halide	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)