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3.3
-
mutant enzyme H257L, in tripart buffer (pH 8.0)
3.5
-
wild type enzyme, in tripart buffer (pH 8.0)
32
-
mutant enzyme H254R, in tripart buffer (pH 8.0)
34
-
mutant enzyme H254R/H257F, in tripart buffer (pH 8.0)
50
-
mutant enzyme H254R/H257L, in tripart buffer (pH 8.0)
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1.9
-
mutant enzyme H257L, in tripart buffer (pH 8.0)
4.2
-
mutant enzyme H254R, in tripart buffer (pH 8.0)
4.4
-
wild type enzyme, in tripart buffer (pH 8.0)
6.2
-
mutant enzyme H254R/H257L, in tripart buffer (pH 8.0)
7.6
-
mutant enzyme H254R/H257F, in tripart buffer (pH 8.0)
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-
Organophosphate hydrolase - an enzyme catalyzing degradation of phosphorus-containing toxins and pesticides
2001
Efremenko, E.N.; Sergeeva, V.S.
Russ. Chem. Bull. (Translation of Izvestiya Akademii Nauk, Seriya Khimicheskaya)
50
1826-1832
-
Purification and characterization of a novel organophosphorus pesticide hydrolase from Penicillium lilacinum BP303
2004
Liu, Y.H.; Liu, Y.; Chen, Z.S.; Lian, J.; Huang, X.; Chung, Y.C.
Enzyme Microb. Technol.
34
297-303
Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX
2007
Ghanem, E.; Li, Y.; Xu, C.; Raushel, F.M.
Biochemistry
46
9032-9040
Balancing the stability and the catalytic specificities of OP hydrolases with enhanced V-agent activities
2008
Reeves, T.E.; Wales, M.E.; Grimsley, J.K.; Li, P.; Cerasoli, D.M.; Wild, J.R.
Protein Eng. Des. Sel.
21
405-412
Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus
2009
Hawwa, R.; Aikens, J.; Turner, R.J.; Santarsiero, B.D.; Mesecar, A.D.
Arch. Biochem. Biophys.
488
109-120
Rhodococcus lactonase with organophosphate hydrolase (OPH) activity and His6-tagged OPH with lactonase activity: evolutionary proximity of the enzymes and new possibilities in their application
2014
Sirotkina, M.; Efremenko, E.N.
Appl. Microbiol. Biotechnol.
98
2647-2656
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