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Literature summary for 3.1.1.75 extracted from

  • Garcia-Hidalgo, J.; Hormigo, D.; Arroyo, M.; de la Mata, I.
    Novel extracellular PHB depolymerase from Streptomyces ascomycinicus: PHB copolymers degradation in acidic conditions (2013), PLoS ONE, 8, e71699.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.75

Activating Compound

Activating Compound Comment Organism Structure
methyl-beta-cyclodextrin
-
 Streptomyces ascomycinicus
PEG 3350
-
 Streptomyces ascomycinicus

Cloned(Commentary)

Cloned (Comment) Organism
gene fkbU, recombinant expression of extracellular wild-type enzyme in Escherichia coli strain BL21(DE3) and Rhodococcus sp. strain T104, the enzyme is secreted, expression of mutants S131A, S131C, D209N, H269E and H269Q in Rhodococcus sp. T104 and secretion to the medium Streptomyces ascomycinicus

Protein Variants

Protein Variants Comment Organism
D209N site-directed mutagenesis, inactive mutant Streptomyces ascomycinicus
H269E site-directed mutagenesis, inactive mutant Streptomyces ascomycinicus
H269Q site-directed mutagenesis, inactive mutant Streptomyces ascomycinicus
S131A site-directed mutagenesis, inactive mutant Streptomyces ascomycinicus
S131C site-directed mutagenesis, inactive mutant Streptomyces ascomycinicus

Inhibitors

Inhibitors Comment Organism Structure
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide/glycinamide 33% inhibition at 5 mM Streptomyces ascomycinicus
2-propanol 71% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
acetone 82% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
acetonitrile 70% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
diethyldicarbonate 40% inhibition at 5 mM, 90% at 20 mM Streptomyces ascomycinicus
diethylene glycol 71% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
DMF 84% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
DMSO 85% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
ethanol 82% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
ethylene glycol 28% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
methanol 91% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
additional information poor inhibition by glycerol. Increase of ionic strength gradually inhibits the poly(3-hydroxybutyrate) depolymerase activity leading to its complete inactivation at 2.5 M NaCl Streptomyces ascomycinicus
NaCl complete inactivation at 2.5 M Streptomyces ascomycinicus
PMSF complete inactivation at 1 mM Streptomyces ascomycinicus
tetrahydrofuran 51% inhibition at 10% (vol/vol) Streptomyces ascomycinicus
triethylene glycol 73% inhibition at 10% (vol/vol) Streptomyces ascomycinicus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Streptomyces ascomycinicus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Streptomyces ascomycinicus
Mg2+ activates Streptomyces ascomycinicus
Mn2+ activates Streptomyces ascomycinicus
additional information enzyme activity is increased in the presence of divalent cations due to non-essential activation Streptomyces ascomycinicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
 1 * 48400, about mass spectrometry, 1 * 48000, SDS-PAGE Streptomyces ascomycinicus
48400
-
 1 * 48400, about mass spectrometry, 1 * 48000, SDS-PAGE Streptomyces ascomycinicus

Organism

Organism UniProt Comment Textmining
Streptomyces ascomycinicus Q9KIF2 sp. nov., gene fkbU
-
Streptomyces ascomycinicus DSM Z 40822 Q9KIF2 sp. nov., gene fkbU
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant extracellular enzyme from Escherichia coli strain BL21(DE3) and Rhodococcus sp. strain T104 by two different steps of hydrophobic interaction chromatography Streptomyces ascomycinicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is able to degrade polyhydroxybutyrate, but also shows ability to degrade films made of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers and a blend of poly(3-hydroxybutyrate) and starch (7:3 proportion wt/wt) Streptomyces ascomycinicus ?
-
 ?
additional information the enzyme is able to degrade polyhydroxybutyrate, but also shows ability to degrade films made of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers and a blend of poly(3-hydroxybutyrate) and starch (7:3 proportion wt/wt) Streptomyces ascomycinicus DSM Z 40822 ?
-
 ?
poly(3-hydroxybutyrate) + H2O average molecular mass of 437 kDa Streptomyces ascomycinicus 3-hydroxybutyrate + 3-hydroxybutyryl-3-hydroxybutyrate
-
 ?
poly(3-hydroxybutyrate) + H2O average molecular mass of 437 kDa Streptomyces ascomycinicus DSM Z 40822 3-hydroxybutyrate + 3-hydroxybutyryl-3-hydroxybutyrate
-
 ?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O substrate co-polymer with 5 or 12% (wt) 3-hydroxyvalerate Streptomyces ascomycinicus ?
-
 ?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O substrate co-polymer with 5 or 12% (wt) 3-hydroxyvalerate Streptomyces ascomycinicus DSM Z 40822 ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 48400, about mass spectrometry, 1 * 48000, SDS-PAGE Streptomyces ascomycinicus
More the enzyme has a globular shape with an alpha-beta hydrolase fold Streptomyces ascomycinicus

Synonyms

Synonyms Comment Organism
PhaZSa
-
 Streptomyces ascomycinicus
PHB depolymerase
-
 Streptomyces ascomycinicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Streptomyces ascomycinicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Streptomyces ascomycinicus

General Information

General Information Comment Organism
additional information the enzyme has a globular shape with an alpha-beta hydrolase fold, three-dimensional structure and homology structure modelling, overview Streptomyces ascomycinicus