Structure and Function Relationships of a Redox-Sensor Protein, Heme-Regulated Phosphodiesterase

التفاصيل البيبلوغرافية
العنوان: Structure and Function Relationships of a Redox-Sensor Protein, Heme-Regulated Phosphodiesterase
المؤلفون: Hirofumi Kurokawa, Yukie Sasakura, Satoshi Hirata, Sue Taguchi, Jotaro Igarashi, M. Watanabe, Ikuko Sagami, Toru Shimizu, Tokiko Suzuki-Yoshimura
المصدر: Seibutsu Butsuri. 45:84-89
بيانات النشر: Biophysical Society of Japan, 2005.
سنة النشر: 2005
مصطلحات موضوعية: chemistry.chemical_classification, Phosphodiesterase, Crystal structure, Redox sensor, Biology, medicine.disease_cause, Structure and function, chemistry.chemical_compound, Enzyme, Biochemistry, chemistry, PAS domain, medicine, Heme, Escherichia coli
الوصف: Heme-regulated phosphodiesterase from Escherichia coli (Ec DOS) is a novel PAS heme-sensor enzyme. Ec DOS is active in the Fe2+ heme-bound form, whereas it is inactive in the Fe3+ heme-bound form. To elucidate the mechanism of the redox-dependent heme-regulated catalysis, we examined spectroscopic and functional characters of site-directed and deletion mutant proteins. We also determined crystal structures of the wild type enzyme under various conditions. In this review, we summarized findings about heme-sensor proteins, PAS domain and phosphodiesterase in general and structure and function relationships of Ec DOS specifically.
تدمد: 1347-4219
0582-4052
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::785eb9800f97ac9ff17b794c2f588217Test
https://doi.org/10.2142/biophys.45.84Test
حقوق: OPEN
رقم الانضمام: edsair.doi...........785eb9800f97ac9ff17b794c2f588217
قاعدة البيانات: OpenAIRE