MODIFICATION OF ARGININE RESIDUES OF L-LYSINE-ALPHA-OXIDASE FROM A TRICHODERMA SPECIES

To investigate the nature of the active site of L-lysine-alpha-oxidase from Trichoderma sp., arginine residues of the enzyme were modified In contrast to L-amino acid oxidase from snake venom, which is completely inactivated, the L-lysine-alpha-oxidase from Trichoderma sp. is irreversibly inactivated by only 18% (the reversible inactivation was 65%) under similar conditions. The data suggest that arginine residues do not play a significant role in the enzymatic activity of the L-lysine-alpha-oxidase.

Авторы
Журнал
Номер выпуска
3
Язык
Английский
Страницы
304-306
Статус
Опубликовано
Том
57
Год
1992
Ключевые слова
L-LYSINE-ALPHA-OXIDASE; TRICHODERMA SP; ACTIVE SITE; MODIFICATION OF ARGININE RESIDUES
Дата создания
19.10.2018
Дата изменения
19.10.2018
Постоянная ссылка
https://repository.rudn.ru/ru/records/article/record/9677/