The effect of cysteine mutations on recombinant deacetoxycephalosporin C synthase from S. clavuligerus.
Cysteines 100, 155, and 197 of recombinant deacetoxycephalosporin C synthase were mutated to alanine residues. The C100A mutant had properties similar to those of the wild-type enzyme, but mutation of Cys-155 and Cys-197 reduced enzyme activity with penicillin N and penicillin G to different extents...
Hlavní autoři: | Lee, H, Lloyd, MD, Harlos, K, Schofield, C |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2000
|
Podobné jednotky
-
Active site mutations of recombinant deacetoxycephalosporin C synthase.
Autor: Lee, H, a další
Vydáno: (2002) -
Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS).
Autor: Lee, H, a další
Vydáno: (2001) -
Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase.
Autor: Dubus, A, a další
Vydáno: (2001) -
Studies on the active site of deacetoxycephalosporin C synthase.
Autor: Lloyd, MD, a další
Vydáno: (1999) -
Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase. The role of arginine 258.
Autor: Lee, H, a další
Vydáno: (2001)