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Literature summary for 3.1.1.76 extracted from

  • Santos, M.; Gangoiti, J.; Keul, H.; Moeller, M.; Serra, J.L.; Llama, M.J.
    Polyester hydrolytic and synthetic activity catalyzed by the medium-chain-length poly(3-hydroxyalkanoate) depolymerase from Streptomyces venezuelae SO1 (2013), Appl. Microbiol. Biotechnol., 97, 211-222.
    View publication on PubMed
Search for more literature for 3.1.1.76

Activating Compound

Activating Compound Comment Organism Structure
2-propanol 2fold activation at 5% (v/v) Streptomyces venezuelae
additional information higher concentrations of detergents show a significant inhibitory effect Streptomyces venezuelae
SDS 3fold activation at 0.01% (w/v) Streptomyces venezuelae
Triton X-100 activates 1.7fold at 0.005% (w/v), inhibits by 72% at 0.03% (w/v) Streptomyces venezuelae
Tween 80 activates1.8fold at 0.005% (w/v), inhibits 90% at 0.01% (w/v) Streptomyces venezuelae

Inhibitors

Inhibitors Comment Organism Structure
Acetic anhydride slight inhibition at 10 mM Streptomyces venezuelae
carbodiimide slight inhibition at 10 mM Streptomyces venezuelae
DTT 69% inhibition at 10 mM, 30% at 1 mM Streptomyces venezuelae
EDTA 73% inhibition at 10 mM Streptomyces venezuelae
iodoacetamide slight inhibition at 10 mM Streptomyces venezuelae
additional information no inhibition by N-ethylmaleimide at 10 mM Streptomyces venezuelae
NaN3 slight inhibition at 10 mM Streptomyces venezuelae
PMSF 40% inhibition at 10 mM Streptomyces venezuelae
Triton X-100 activates 1.7fold at 0.005% (w/v), inhibits by 72% at 0.03% (w/v) Streptomyces venezuelae
Tween 80 activates1.8fold at 0.005% (w/v), inhibits 90% at 0.01% (w/v) Streptomyces venezuelae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.122
-
 4-nitrophenyl octanoate pH 9.0, 37°C Streptomyces venezuelae

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
 x * 27000, SDS-PAGE Streptomyces venezuelae

Organism

Organism UniProt Comment Textmining
Streptomyces venezuelae
-
 isolated from a soil sample taken at the Campus of the University of the Basque Country, Bizkaia, Spain
-
Streptomyces venezuelae SO1
-
 isolated from a soil sample taken at the Campus of the University of the Basque Country, Bizkaia, Spain
-

Purification (Commentary)

Purification (Comment) Organism
extracellualr enzyme 4.2fold to homogeneity Streptomyces venezuelae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12.1
-
 purified enzyme, pH 9.5, 30°C, substrate poly(3-hydroxyoctanoate-co-3-hydroxyhexanoate) Streptomyces venezuelae

Storage Stability

Storage Stability Organism
-20 to -80°C, purified enzyme, 85% activity remaining after 6 months Streptomyces venezuelae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl decanoate + H2O high activity Streptomyces venezuelae ?
-
 ?
4-nitrophenyl decanoate + H2O high activity Streptomyces venezuelae SO1 ?
-
 ?
4-nitrophenyl dodecanoate + H2O high activity Streptomyces venezuelae ?
-
 ?
4-nitrophenyl dodecanoate + H2O high activity Streptomyces venezuelae SO1 ?
-
 ?
4-nitrophenyl hexadecanoate + H2O lower activity Streptomyces venezuelae ?
-
 ?
4-nitrophenyl hexadecanoate + H2O lower activity Streptomyces venezuelae SO1 ?
-
 ?
4-nitrophenyl octanoate + H2O best artificial substrate, the enzyme can hydrolyze various substrates for esterases, such as tributyrin and 4-nitrophenyl-alkanoates Streptomyces venezuelae ?
-
 ?
4-nitrophenyl valerate + H2O
-
 Streptomyces venezuelae ?
-
 ?
additional information the enzyme catalyzes the hydrolysis of poly-3-hydroxyoctanoate to monomeric units and the ring-opening polymerization of beta-butyrolactone and lactides, while epsilon-caprolactone and pentadecalactone are hardly polymerized, the enzyme shows esterase activity with tributyrin as substrate. It is unable of hydrolysing olive oil, and shows poor activity with 4-nitrophenyl esteras of acetate, butyrate, and octadecanoate Streptomyces venezuelae ?
-
 ?
additional information the enzyme catalyzes the hydrolysis of poly-3-hydroxyoctanoate to monomeric units and the ring-opening polymerization of beta-butyrolactone and lactides, while epsilon-caprolactone and pentadecalactone are hardly polymerized, the enzyme shows esterase activity with tributyrin as substrate. It is unable of hydrolysing olive oil, and shows poor activity with 4-nitrophenyl esteras of acetate, butyrate, and octadecanoate Streptomyces venezuelae SO1 ?
-
 ?
poly(3-hydroxyoctanoate-co-3-hydroxyhexanoate) + H2O latex suspension Streptomyces venezuelae (R)-3-hydroxyoctanoate + ? the monomer of 3-hydroxyoctanoate and the trimer are detected as the main hydrolysis products, representing 28 and 35% of the total degradation products, respectively. Additionally, dimers as well as the trimer are also detected as minor products, longer periods of incubation increase the concentration of the monomer, whereas that of trimers decreases markedly ?
poly(3-hydroxyoctanoate-co-3-hydroxyhexanoate) + H2O latex suspension Streptomyces venezuelae SO1 (R)-3-hydroxyoctanoate + ? the monomer of 3-hydroxyoctanoate and the trimer are detected as the main hydrolysis products, representing 28 and 35% of the total degradation products, respectively. Additionally, dimers as well as the trimer are also detected as minor products, longer periods of incubation increase the concentration of the monomer, whereas that of trimers decreases markedly ?

Subunits

Subunits Comment Organism
? x * 27000, SDS-PAGE Streptomyces venezuelae

Synonyms

Synonyms Comment Organism
MCL-PHA depolymerase
-
 Streptomyces venezuelae
medium-chain-length poly(3-hydroxyalkanoate) depolymerase
-
 Streptomyces venezuelae
medium-chain-length polyhydroxyalkanoate depolymerase
-
 Streptomyces venezuelae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Streptomyces venezuelae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 thermal inactivation of the enzyme followed first-order kinetics in all cases, a value of 48.7 kcal/mol is calculated for the activation energy of enzyme thermal inactivation Streptomyces venezuelae
30
-
 purified enzyme, retains full initial activity after 24 h Streptomyces venezuelae
40
-
 purified enzyme, retains 80% of its initial activity after 8 h Streptomyces venezuelae
45
-
 purified enzyme, retains 50% of its initial activity after 8 h Streptomyces venezuelae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.5 maximum activity in the alkaline pH-range Streptomyces venezuelae

pH Range

pH Minimum pH Maximum Comment Organism
7.5 11 over 60% of maximal activity within this range Streptomyces venezuelae

pI Value

Organism Comment pI Value Maximum pI Value
Streptomyces venezuelae isoelectric focusing
-
 5.9