Histidine-15 and lytic activity of lysozyme.
J Biosci
;
1991 June; 16(1&2): 21-28
Artículo
en Inglés
| IMSEAR
| ID: sea-160742
ABSTRACT
The literature data on the activity of histidine-15 modified hen egg white lysozyme are conflicting the modified enzyme is reported to have more activity, similar activity or less activity by different authors. Amino acid analysis had shown modification of the single His-15. Detailed activity studies on His-15-modified (by iodoacetic acid or diethyl pyrocarbonate) lysozyme have shown that the contradicting reports are due to the specific choices of ionic strengths and cell wall substrate concentrations and can be attributed to the substrate being negatively charged. Our analysis suggests that even though histidine-15 is far removed from the active site of lysozyme, its chemical modification or binding of the negatively-charged substrate near it, changes the conformation around the active site. However, the change in the optimum activity on chemically modifying His-15 is small.
Texto completo:
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Índice:
IMSEAR (Asia Sudoriental)
Idioma:
Inglés
Revista:
J Biosci
Año:
1991
Tipo del documento:
Artículo
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