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Literature summary for 3.8.1.5 extracted from

  • Zhao, Y.Z.; Yu, W.L.; Zheng, H.; Guo, X.; Guo, N.; Hu, T.; Zhong, J.Y.
    PEGylation with the thiosuccinimido butylamine linker significantly increases the stability of haloalkane dehalogenase DhaA (2017), J. Biotechnol., 254, 25-33 .
    View publication on PubMed
Search for more literature for 3.8.1.5

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Rhodococcus rhodochrous

General Stability

General Stability Organism
enzyme PEGylated with the thiosuccinimido butylamine linker shows the maximum resistance to high ionic strength (1 M NaCl) Rhodococcus rhodochrous
PEGylation with the thiosuccinimido butylamine linker significantly increases the stability of the enzyme Rhodococcus rhodochrous

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, wild-type enzyme Rhodococcus rhodochrous
4.9
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker Rhodococcus rhodochrous
6.9
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker Rhodococcus rhodochrous

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 SDS-PAGE Rhodococcus rhodochrous

Organic Solvent Stability

Organic Solvent Comment Organism
DMSO the remaining activity of wild-type enzyme (DhaA) is 15.4% in 40% (v/v) DMSO solution at 37 °C. The remaining activity of the enzyme mono-PEGylated with the thiosuccinimido butylamine linker is 37.4% and the remaining activity of the enzyme multi-PEGylated enzyme with the thiosuccinimido butylamine linker is 48.5% Rhodococcus rhodochrous

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous P0A3G2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rhodococcus rhodochrous

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bis(2-chloroethyl) ether + H2O
-
 Rhodococcus rhodochrous ?
-
 ?

Subunits

Subunits Comment Organism
? x * 35000, SDS-PAGE Rhodococcus rhodochrous

Synonyms

Synonyms Comment Organism
DhaA
-
 Rhodococcus rhodochrous

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 PEGylation with the thiosuccinimido butylamine linker significantly increases the thermal stability of the enzyme Rhodococcus rhodochrous

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker Rhodococcus rhodochrous
0.08
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker Rhodococcus rhodochrous
0.11
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, wild-type enzyme Rhodococcus rhodochrous

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 9 multi-PEGylated enzyme with the thiosuccinimido butylamine linker and mono-PEGylated enzyme with the thiosuccinimido butylamine linker show the remaining activities comparable to wild-type enzyme Rhodococcus rhodochrous

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.007
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker Rhodococcus rhodochrous
0.016
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker Rhodococcus rhodochrous
0.04
-
 bis(2-chloroethyl) ether 37°C, pH 8.2, wild-type enzyme Rhodococcus rhodochrous