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Literature summary for 3.1.1.76 extracted from

  • Papaneophytou, C.; Velali, E.; Pantazaki, A.
    Purification and characterization of an extracellular medium-chain length polyhydroxyalkanoate depolymerase from Thermus thermophilus HB8 (2011), Polym. Degrad. Stab., 96, 670-678.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
acetone
-
Thermus thermophilus
methanol
-
Thermus thermophilus
additional information no effect by 2-mercaptoethanol Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
ethanol slight inhibition Thermus thermophilus
additional information no effect by 2-mercaptoethanol on enzyme activity Thermus thermophilus
PMSF
-
Thermus thermophilus
Triton X-100 inhibition at high concentration Thermus thermophilus
Tween 20 inhibition at high concentration Thermus thermophilus
Tween 80 inhibition at high concentration Thermus thermophilus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Thermus thermophilus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
x * 28000, SDS-PAGE Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
poly(3-hydroxydecanoate-co-3-hydroxhyoctanoate) + H2O Thermus thermophilus
-
?
-
?
poly(3-hydroxydecanoate-co-3-hydroxhyoctanoate) + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
?
-
?
poly(3-hydroxyoctanoic acid) + H2O Thermus thermophilus
-
?
-
?
poly(3-hydroxyoctanoic acid) + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
?
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
the enzyme is encoded in parts of gene TTHA1605
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the enzyme is encoded in parts of gene TTHA1605
-

Purification (Commentary)

Purification (Comment) Organism
the enzyme is purified from cell medium 10.4fold by acetone precipitation, hydrophobic interaction chromatography using Octyl-Sepharose CL-4B, and gel filtration to homogeneity Thermus thermophilus

Source Tissue

Source Tissue Comment Organism Textmining
additional information cell growth on sodium octanoate Thermus thermophilus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl octanoate + H2O
-
Thermus thermophilus octanoate + 4-nitrophenol
-
?
4-nitrophenyl octanoate + H2O
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 octanoate + 4-nitrophenol
-
?
additional information substrate specificity, overview, the extracellular mcl-PHA depolymerase is also capable of hydrolyzing various short- and medium-chain length 4-nitrophenyl-alkanoates, no activity with poly(3-hydroxybutyrate) Thermus thermophilus ?
-
?
additional information substrate specificity, overview, the extracellular mcl-PHA depolymerase is also capable of hydrolyzing various short- and medium-chain length 4-nitrophenyl-alkanoates, no activity with poly(3-hydroxybutyrate) Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
poly(3-hydroxydecanoate-co-3-hydroxhyoctanoate) + H2O
-
Thermus thermophilus ?
-
?
poly(3-hydroxydecanoate-co-3-hydroxhyoctanoate) + H2O
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
poly(3-hydroxyoctanoic acid) + H2O
-
Thermus thermophilus ?
-
?
poly(3-hydroxyoctanoic acid) + H2O
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?

Subunits

Subunits Comment Organism
? x * 28000, SDS-PAGE Thermus thermophilus

Synonyms

Synonyms Comment Organism
MCL-PHA depolymerase
-
Thermus thermophilus
medium-chain length polyhydroxyalkanoate depolymerase
-
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
with substrate 4-nitrophenyl octanoate Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Thermus thermophilus

pH Range

pH Minimum pH Maximum Comment Organism
6 11 the purified enzyme is most active at pH range of pH 7.0-9.0, while the maximal activity is observed at pH 8.5. At pH 6.0 and pH 11 the enzyme shows 34% and 7.5% of maximal activity, respectively Thermus thermophilus

General Information

General Information Comment Organism
additional information the mcl-PHA depolymerase from Thermus thermophilus is a distinct enzyme, which is different from those of other mcl-PHAdegrading bacteria Thermus thermophilus