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Literature summary for 3.1.1.75 extracted from

  • Tseng, C.L.; Chen, H.J.; Shaw, G.C.
    Identification and characterization of the Bacillus thuringiensis phaZ gene, encoding new intracellular poly-3-hydroxybutyrate depolymerase (2006), J. Bacteriol., 188, 7592-7599.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.75

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged PhaZ and its variant in Escherichia coli JM109 Bacillus thuringiensis

Protein Variants

Protein Variants Comment Organism
S102A mutant without poly[(R)-3-hydroxybutanoate]n hydrolyzing activity Bacillus thuringiensis

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
 Bacillus thuringiensis 5622
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
poly[(R)-3-hydroxybutanoate]n + H2O Bacillus thuringiensis PhaZ can function as a PHB depolymerase in vivo poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
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 subsp. israelensis ATCC 35646
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Purification (Commentary)

Purification (Comment) Organism
purification of His-tagged PhaZ and its variant in Escherichia coli JM109 Bacillus thuringiensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information inactive against p-nitrophenylpalmitate, tributyrin, and triolein Bacillus thuringiensis ?
-
 ?
p-nitrophenyl butyrate + H2O
-
 Bacillus thuringiensis p-nitrophenol + butyrate
-
 ?
p-nitrophenyl laurate + H2O
-
 Bacillus thuringiensis p-nitrophenol + laurate
-
 ?
p-nitrophenyldecanoate + H2O
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 Bacillus thuringiensis p-nitrophenol + decanoate
-
 ?
poly[(R)-3-hydroxybutanoate]n + H2O PhaZ can function as a PHB depolymerase in vivo Bacillus thuringiensis poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
 ?
poly[(R)-3-hydroxybutanoate]n + H2O purified His-tagged PhaZ can efficiently degrade trypsin-activated native poly-3-hydroxybutyrate granules as well as artificial amorphous poly-3-hydroxybutyrate granules and release 3-hydroxybutyrate monomer as a hydrolytic product, but it can not hydrolyze denatured semicrystalline poly-3-hydroxybutyrate Bacillus thuringiensis poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
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 ?