Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification
Takatoshi Arakawa
1
,
Yoshiaki Kawano
1
,
Yoko Katayama
1
,
HIROSHI NAKAYAMA
1
,
NAOSHI DOHMAE
1
,
Masafumi Yohda
1
,
Masafumi Odaka
1
Тип публикации: Journal Article
Дата публикации: 2009-09-28
scimago Q1
wos Q1
БС1
SJR: 5.554
CiteScore: 22.5
Impact factor: 15.6
ISSN: 00027863, 15205126
PubMed ID:
19785438
General Chemistry
Catalysis
Biochemistry
Colloid and Surface Chemistry
Краткое описание
Thiocyanate hydrolase (SCNase) is a member of a family of nitrile hydratase proteins, each of which contains a unique noncorrin cobalt center with two post-translationally modified cysteine ligands, cysteine-sulfenic acid or -sulfenate (Cys-SO(H)), and cysteine-sulfininate (Cys-SO(2)(-)), respectively. We have found that a partially matured recombinant SCNase was activated during storage. The crystal structures of SCNase before and after storage demonstrated that Cys-SO(2)(-) modification of gammaCys131 proceeded to completion prior to storage, while Cys-SO(H) modification of gammaCys133 occurred during storage. SCNase activity was suppressed when gammaCys133 was further oxidized to Cys-SO(2)(-). The correlation between the catalytic activity and the extent of the gammaCys133 modification indicates that the cysteine sulfenic acid modification of gammaCys133 is of primary importance in determining the activity of SCNase.
Найдено
Ничего не найдено, попробуйте изменить настройки фильтра.
Найдено
Ничего не найдено, попробуйте изменить настройки фильтра.
Топ-30
Журналы
|
1
2
3
4
5
6
|
|
|
Inorganic Chemistry
6 публикаций, 14.63%
|
|
|
Journal of the American Chemical Society
3 публикации, 7.32%
|
|
|
Journal of Biological Inorganic Chemistry
2 публикации, 4.88%
|
|
|
Journal of Biological Chemistry
2 публикации, 4.88%
|
|
|
Biochemistry
2 публикации, 4.88%
|
|
|
Catalysts
1 публикация, 2.44%
|
|
|
Scientific Reports
1 публикация, 2.44%
|
|
|
PLoS ONE
1 публикация, 2.44%
|
|
|
Free Radical Biology and Medicine
1 публикация, 2.44%
|
|
|
Biochemical and Biophysical Research Communications
1 публикация, 2.44%
|
|
|
Journal of Fluorine Chemistry
1 публикация, 2.44%
|
|
|
Journal of Bioscience and Bioengineering
1 публикация, 2.44%
|
|
|
Inorganic Chemistry Communication
1 публикация, 2.44%
|
|
|
Angewandte Chemie
1 публикация, 2.44%
|
|
|
Angewandte Chemie - International Edition
1 публикация, 2.44%
|
|
|
European Journal of Organic Chemistry
1 публикация, 2.44%
|
|
|
Mass Spectrometry Reviews
1 публикация, 2.44%
|
|
|
Chemical Reviews
1 публикация, 2.44%
|
|
|
Journal of Proteome Research
1 публикация, 2.44%
|
|
|
Journal of Physical Chemistry B
1 публикация, 2.44%
|
|
|
ACS Catalysis
1 публикация, 2.44%
|
|
|
Crystallography Reports
1 публикация, 2.44%
|
|
|
Proceedings of the National Academy of Sciences of the United States of America
1 публикация, 2.44%
|
|
|
Plant, Cell and Environment
1 публикация, 2.44%
|
|
|
Biochemistry (Moscow)
1 публикация, 2.44%
|
|
|
Journal of Coordination Chemistry
1 публикация, 2.44%
|
|
|
Molecular Catalysis
1 публикация, 2.44%
|
|
|
Russian Chemical Reviews
1 публикация, 2.44%
|
|
|
ACS Central Science
1 публикация, 2.44%
|
|
|
1
2
3
4
5
6
|
Издатели
|
2
4
6
8
10
12
14
16
|
|
|
American Chemical Society (ACS)
16 публикаций, 39.02%
|
|
|
Elsevier
6 публикаций, 14.63%
|
|
|
Wiley
6 публикаций, 14.63%
|
|
|
Springer Nature
3 публикации, 7.32%
|
|
|
American Society for Biochemistry and Molecular Biology
2 публикации, 4.88%
|
|
|
Pleiades Publishing
2 публикации, 4.88%
|
|
|
MDPI
1 публикация, 2.44%
|
|
|
Public Library of Science (PLoS)
1 публикация, 2.44%
|
|
|
Cold Spring Harbor Laboratory
1 публикация, 2.44%
|
|
|
Proceedings of the National Academy of Sciences (PNAS)
1 публикация, 2.44%
|
|
|
Taylor & Francis
1 публикация, 2.44%
|
|
|
Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii
1 публикация, 2.44%
|
|
|
2
4
6
8
10
12
14
16
|
- Мы не учитываем публикации, у которых нет DOI.
- Статистика публикаций обновляется еженедельно.
Вы ученый?
Создайте профиль, чтобы получать персональные рекомендации коллег, конференций и новых статей.
Метрики
41
Всего цитирований:
41
Цитирований c 2024:
6
(14.64%)
Цитировать
ГОСТ |
RIS |
BibTex |
MLA
Цитировать
ГОСТ
Скопировать
Arakawa T. et al. Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification // Journal of the American Chemical Society. 2009. Vol. 131. No. 41. pp. 14838-14843.
ГОСТ со всеми авторами (до 50)
Скопировать
Arakawa T., Kawano Y., Katayama Y., NAKAYAMA H., DOHMAE N., Yohda M., Odaka M. Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification // Journal of the American Chemical Society. 2009. Vol. 131. No. 41. pp. 14838-14843.
Цитировать
RIS
Скопировать
TY - JOUR
DO - 10.1021/ja903979s
UR - https://doi.org/10.1021/ja903979s
TI - Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification
T2 - Journal of the American Chemical Society
AU - Arakawa, Takatoshi
AU - Kawano, Yoshiaki
AU - Katayama, Yoko
AU - NAKAYAMA, HIROSHI
AU - DOHMAE, NAOSHI
AU - Yohda, Masafumi
AU - Odaka, Masafumi
PY - 2009
DA - 2009/09/28
PB - American Chemical Society (ACS)
SP - 14838-14843
IS - 41
VL - 131
PMID - 19785438
SN - 0002-7863
SN - 1520-5126
ER -
Цитировать
BibTex (до 50 авторов)
Скопировать
@article{2009_Arakawa,
author = {Takatoshi Arakawa and Yoshiaki Kawano and Yoko Katayama and HIROSHI NAKAYAMA and NAOSHI DOHMAE and Masafumi Yohda and Masafumi Odaka},
title = {Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification},
journal = {Journal of the American Chemical Society},
year = {2009},
volume = {131},
publisher = {American Chemical Society (ACS)},
month = {sep},
url = {https://doi.org/10.1021/ja903979s},
number = {41},
pages = {14838--14843},
doi = {10.1021/ja903979s}
}
Цитировать
MLA
Скопировать
Arakawa, Takatoshi, et al. “Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification.” Journal of the American Chemical Society, vol. 131, no. 41, Sep. 2009, pp. 14838-14843. https://doi.org/10.1021/ja903979s.