Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.75 extracted from

  • Numata, K.; Yamashita, K.; Fujita, M.; Tsuge, T.; Kasuya, K.; Iwata, T.; Doi, Y.; Abe, H.
    Adsorption and hydrolysis reactions of poly(hydroxybutyric acid) depolymerases secreted from Ralstonia pickettii T1 and Penicillium funiculosum onto poly[(R)-3-hydroxybutyric acid] (2007), Biomacromolecules, 8, 2276-2281.
    View publication on PubMed
Search for more literature for 3.1.1.75

Organism

Organism UniProt Comment Textmining
Ralstonia pickettii
-
-
-
Ralstonia pickettii T1
-
-
-
Talaromyces funiculosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Ralstonia pickettii
-
 Talaromyces funiculosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information adsorption of single molecules of the PHB depolymerase onto poly[(R)-3-hydroxybutyric acid] single crystals and the degradation of the single crystals in a phosphate buffer solution at 37°C by real-time atomic force microscopy is observed Ralstonia pickettii ?
-
 ?
additional information the enzymes is adsorbed onto the surface of poly[(R)-3-hydroxybutyric acid] single crystals Talaromyces funiculosus ?
-
 ?
additional information adsorption of single molecules of the PHB depolymerase onto poly[(R)-3-hydroxybutyric acid] single crystals and the degradation of the single crystals in a phosphate buffer solution at 37°C by real-time atomic force microscopy is observed Ralstonia pickettii T1 ?
-
 ?

Subunits

Subunits Comment Organism
More the PHB depolymerase from Ralstonia pickettii T1 consists of catalytic, linker, and substrate-binding domains Ralstonia pickettii