Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Jane M. Kuo"'
Publikováno v:
Proteins: Structure, Function, and Genetics. 29:553-561
Phosphotriesterase (PTE) is a zinc metalloenzyme that catalyzes the hydro- lysis of an extensive array of organophosphate pesticides and mammalian acetylcholinester- ase nerve agents. Although the three-dimen- sional crystal structure of PTE has been
Publikováno v:
Journal of Biological Chemistry. 272:8857-8860
The covalently bound prosthetic group of lactoperoxidase (LPO) has been obtained by hydrolysis of the protein and identified as a dihydroxylated heme. A baculovirus expression system has been developed for LPO and used to obtain protein in which the
Publikováno v:
Biochemistry. 34:750-754
The alkynyl phosphate ester, 1-hexynyl diethyl phosphate (I), is a mechanism-based inhibitor of phosphotriesterase. It has been previously determined that a histidine residue in the wild-type phosphotriesterase is covalently modified by this compound
Publikováno v:
Journal of the American Chemical Society. 116:5529-5533
Publikováno v:
Journal of Biological Chemistry. 267:13278-13283
The bacterial phosphotriesterase has been found to require a divalent cation for enzymatic activity. This enzyme catalyzes the detoxification of organophosphorus insecticides and nerve agents. In an Escherichia coli expression system significantly hi
Publikováno v:
The Journal of biological chemistry. 277(9)
The heme in lactoperoxidase is attached to the protein by ester bonds between the heme 1- and 5-methyl groups and Glu-375 and Asp-275, respectively. To investigate the cross-linking process, we have examined the D225E, E375D, and D225E/E375D mutants
Publikováno v:
Biochemistry. 37(30)
To examine the role of Arg38 in the peroxidative and peroxygenative activity of horseradish peroxidase (HRP), we have expressed the R38A, R38H, and R38H/H42V mutants. The R38A HRP mutant gives a normal compound I species with H2O2 that is reduced by
Publikováno v:
Biochemistry. 36(8)
Phosphotriesterase catalyzes the hydrolysis of organophosphate nerve agents. Four amino acid residues, located within the active site pocket, were mutated in an effort to ascertain the roles that these groups play in the structure and function of thi
Publikováno v:
Biochemistry. 34(25)
Phosphotriesterase, as isolated from Pseudomonas diminuta, is capable of detoxifying widely used pesticides such as paraoxon and parathion and various mammalian acetylcholinesterase inhibitors. The enzyme requires a binuclear metal center for activit
Autor:
David R. Fischer, Jane M. Kuo, Bryant W. Miles, Jennifer A. Banzon, Peter J. Stang, Frank M. Raushel
Publikováno v:
Biochemistry. 34(3)
Five alkynyl phosphate esters have been synthesized as probes of the active site structure of phosphotriesterase. These compounds have the potential to be converted by the enzyme to a highly reactive ketene intermediate which can then react with an a