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Literature summary for 3.1.1.76 extracted from

  • Martinez, V.; de la Pena, F.; Garcia-Hidalgo, J.; de la Mata, I.; Garcia, J.L.; Prieto, M.A.
    Identification and biochemical evidence of a medium-chain-length polyhydroxyalkanoate depolymerase in the Bdellovibrio bacteriovorus predatory hydrolytic arsenal (2012), Appl. Environ. Microbiol., 78, 6017-6026.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.76

Activating Compound

Activating Compound Comment Organism Structure
EDTA 10% activation at 10 mM Bdellovibrio bacteriovorus
sodium cholate 30% activation at 0.02 mM, 18% at 0.2 mM Bdellovibrio bacteriovorus

Application

Application Comment Organism
synthesis the enzyme migt be used as biocatalyst for the production of enantiopure hydroxyalkanoic acids and oligomers as building blocks for the synthesis of biobased polymers Bdellovibrio bacteriovorus

Cloned(Commentary)

Cloned (Comment) Organism
orf Bd3709, recombinant extracellular expression in different hypersecretor Tol-pal mutant strains of Escherichia coli and Pseudomonas putida, e.g. in Escherichia coli strain DH10B(pIZBd1) periplasm or Pseudomonas putida strain KT2442, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)(pETBd1) Bdellovibrio bacteriovorus

Inhibitors

Inhibitors Comment Organism Structure
cetyltrimethylammonium bromide 88% inhibition at 0.05 vol% Bdellovibrio bacteriovorus
deoxycholate 84% inhibition at 0.05 vol% Bdellovibrio bacteriovorus
dithiothreitol 45% inhibition at 10 mM DTT Bdellovibrio bacteriovorus
additional information not affected by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide treatment, and by 1 mM cyclodextrin Bdellovibrio bacteriovorus
phenylmethylsulfonyl fluoride 10% inhibition at 1 mM, 90% inhibition at 10 mM Bdellovibrio bacteriovorus
SDS 47% inhibition at 0.05 vol% Bdellovibrio bacteriovorus
sodium cholate 57% inhibition at 2 mM Bdellovibrio bacteriovorus
Triton X-100 90% inhibition at 0.01 vol% Bdellovibrio bacteriovorus
Tween 80 92% inhibition at 0.05 vol%, 79% inhibition at 0.005 vol% Bdellovibrio bacteriovorus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bdellovibrio bacteriovorus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no effect by 1 mM MgCl2 or CaCl2 Bdellovibrio bacteriovorus
NaCl a high ionic strength of 0.5 M NaCl in the reaction mixture is required for optimal activity Bdellovibrio bacteriovorus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bdellovibrio bacteriovorus the enzyme is an endoexohydrolase that cleaves both large and small polyhydroxyalkanoate molecules, producing mainly dimers but also monomers and trimers. The enzyme specifically degrades medium-chain-length polyhydroxyalkanoates and is inactive toward short-chain-length polyhydroxyalkanoates like polyhydroxybutyrate ?
-
 ?
additional information Bdellovibrio bacteriovorus HD100 the enzyme is an endoexohydrolase that cleaves both large and small polyhydroxyalkanoate molecules, producing mainly dimers but also monomers and trimers. The enzyme specifically degrades medium-chain-length polyhydroxyalkanoates and is inactive toward short-chain-length polyhydroxyalkanoates like polyhydroxybutyrate ?
-
 ?
polyhydroxyalkanoate latex + H2O Bdellovibrio bacteriovorus
-
 ?
-
 ?
polyhydroxyalkanoate latex + H2O Bdellovibrio bacteriovorus HD100
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bdellovibrio bacteriovorus
-
 orf Bd3709
-
Bdellovibrio bacteriovorus HD100
-
 orf Bd3709
-

Purification (Commentary)

Purification (Comment) Organism
recombinant extracellular enzyme by hydrophobic interaction chromatography, recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)(pETBd1) by nickel affinity chromatography Bdellovibrio bacteriovorus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
55 560 purified recombinant His-tagged enzme, pH 8.0, 37°C, different assay methods Bdellovibrio bacteriovorus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is an endoexohydrolase that cleaves both large and small polyhydroxyalkanoate molecules, producing mainly dimers but also monomers and trimers. The enzyme specifically degrades medium-chain-length polyhydroxyalkanoates and is inactive toward short-chain-length polyhydroxyalkanoates like polyhydroxybutyrate Bdellovibrio bacteriovorus ?
-
 ?
additional information the enzyme is an endoexohydrolase that cleaves both large and small polyhydroxyalkanoate molecules, producing mainly dimers but also monomers and trimers. The enzyme specifically degrades medium-chain-length polyhydroxyalkanoates and is inactive toward short-chain-length polyhydroxyalkanoates like polyhydroxybutyrate Bdellovibrio bacteriovorus HD100 ?
-
 ?
polyhydroxyalkanoate latex + H2O
-
 Bdellovibrio bacteriovorus ?
-
 ?
polyhydroxyalkanoate latex + H2O
-
 Bdellovibrio bacteriovorus HD100 ?
-
 ?

Synonyms

Synonyms Comment Organism
extracellular MCL-PHA depolymerase
-
 Bdellovibrio bacteriovorus
MCL-PHA depolymerase
-
 Bdellovibrio bacteriovorus
medium-chain-length polyhydroxyalkanoate depolymerase
-
 Bdellovibrio bacteriovorus
PhaZBd
-
 Bdellovibrio bacteriovorus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Bdellovibrio bacteriovorus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 50 activity range, highly active at 4-45°C, 29% of maximal activityy at 50°C Bdellovibrio bacteriovorus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Bdellovibrio bacteriovorus

pH Range

pH Minimum pH Maximum Comment Organism
5 11 activity range, almost inactive at pH 12.0 Bdellovibrio bacteriovorus

General Information

General Information Comment Organism
evolution the enzyme belongs to the alpha/beta-hydrolase fold family Bdellovibrio bacteriovorus
additional information the enzyme has a typical serine hydrolase catalytic triad, serine-histidine-aspartic acid Bdellovibrio bacteriovorus