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Literature summary for 3.1.1.75 extracted from

  • Tan, L.T.; Hiraishi, T.; Sudesh, K.; Maeda, M.
    Effects of mutation at position 285 of Ralstonia pickettii T1 poly[(R)-3-hydroxybutyrate] depolymerase on its activities (2014), Appl. Microbiol. Biotechnol., 98, 7061-7068.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information the poly((R)-3-hydroxybutyrate)-degrading activities of N285X are reciprocally related to their pNPCn-hydrolyzing activities, with the exception of N285A and N285G, and that His residue could functionally substitute for Asn285 on poly((R)-3-hydroxybutyrate) degradation. Among the mutant enzymes, N285E displays the highest hydrolysis rate regardless of substrate concentration or carbon chain length. N285A has comparable hydrolysis rates to N285E at low substrate concentrations (0.1-0.4 mM) for all the substrates regardless of carbon chain lengths. N285H shows one of the lowest hydrolysis rates among the mutant enzymes regardless of substrate concentration or carbon chain length Ralstonia pickettii
N285A site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6 Ralstonia pickettii
N285D site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6 Ralstonia pickettii
N285E site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6 Ralstonia pickettii
N285G site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6 Ralstonia pickettii
N285H site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6 Ralstonia pickettii
N285Y site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6 Ralstonia pickettii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of wild-type and mutant enzymes, overview Ralstonia pickettii

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
Ralstonia pickettii 4-nitrophenol + acetate
-
?
4-nitrophenyl acetate + H2O
-
Ralstonia pickettii T1 4-nitrophenol + acetate
-
?
4-nitrophenyl butyrate + H2O
-
Ralstonia pickettii 4-nitrophenol + butyrate
-
?
4-nitrophenyl butyrate + H2O
-
Ralstonia pickettii T1 4-nitrophenol + butyrate
-
?
4-nitrophenyl hexanoate + H2O
-
Ralstonia pickettii 4-nitrophenol + hexanoate
-
?
4-nitrophenyl hexanoate + H2O
-
Ralstonia pickettii T1 4-nitrophenol + hexanoate
-
?
4-nitrophenyl propionate + H2O
-
Ralstonia pickettii 4-nitrophenol + propionate
-
?
4-nitrophenyl propionate + H2O
-
Ralstonia pickettii T1 4-nitrophenol + propionate
-
?
4-nitrophenyl valerate + H2O
-
Ralstonia pickettii 4-nitrophenol + valerate
-
?
4-nitrophenyl valerate + H2O
-
Ralstonia pickettii T1 4-nitrophenol + valerate
-
?
poly((R)-3-hydroxybutyrate) + H2O
-
Ralstonia pickettii ?
-
?

Synonyms

Synonyms Comment Organism
PhaZRpiT1
-
Ralstonia pickettii
PHB depolymerase
-
Ralstonia pickettii
poly[(R)-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