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Literature summary for 3.1.1.75 extracted from

  • Hiraishi, T.; Komiya, N.; Matsumoto, N.; Abe, H.; Fujita, M.; Maeda, M.
    Degradation and adsorption characteristics of PHB depolymerase as revealed by kinetics of mutant enzymes with amino acid substitution in substrate-binding domain (2010), Biomacromolecules, 11, 113-119.
    View publication on PubMed
Search for more literature for 3.1.1.75

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Ralstonia pickettii

Protein Variants

Protein Variants Comment Organism
L441H CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. L441H and Y443H enzymes have lower poly((R)-3-hydroxybutyrate)-degrading activity than their wild-type counterpart. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface Ralstonia pickettii
S445C CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. S445C has higher poly((R)-3-hydroxybutyrate)-degrading activity than wild-type. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface Ralstonia pickettii
Y443H CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. L441H and Y443H enzymes have lower poly((R)-3-hydroxybutyrate)-degrading activity than their wild-type counterpart. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface Ralstonia pickettii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Ralstonia pickettii
-
-

Organism

Organism UniProt Comment Textmining
Ralstonia pickettii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly((R)-3-hydroxybutyrate) + H2O
-
 Ralstonia pickettii ?
-
 ?

Synonyms

Synonyms Comment Organism
poly(3-hydroxybutyrate) depolymerase
-
 Ralstonia pickettii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Ralstonia pickettii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Ralstonia pickettii