Literature summary for 3.1.1.75 extracted from

Hiraishi, T.; Hirahara, Y.; Doi, Y.; Maeda, M.; Taguchi, S.
Effects of mutations in the substrate-binding domain of poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation (2006), Appl. Environ. Microbiol., 72, 7331-7338.

Search for more literature for 3.1.1.75

Protein Variants

Protein Variants	Comment	Organism
L441H	mutant enzyme with lower degradation of denatured poly(R)-3-hydroxybutyrate and adsorption abilities. Lowering the affinity of the substrate-binding domain towards denatured poly(R)-3-hydroxybutyrate causes a decrease in the degradation rate without the loss of its hydrolytic activity for the polymer chain	Ralstonia pickettii

Organism

Organism	UniProt	Comment	Textmining
Ralstonia pickettii	P12625	precursor	-
Ralstonia pickettii T1	P12625	precursor	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type and mutant enzyme L441H	Ralstonia pickettii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[(R)-3-hydroxybutanoate]n + H2O	-	Ralstonia pickettii	[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]	-	?
[(R)-3-hydroxybutanoate]n + H2O	-	Ralstonia pickettii T1	[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]	-	?

Synonyms

Synonyms	Comment	Organism
PhaZRpiT1	-	Ralstonia pickettii

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)