Four thiol-oxidoreductases involved in the formation of disulphide bonds in the Streptomyces lividans TK21 secretory proteins
Abstract Background Bacterial secretory proteins often require the formation of disulphide bonds outside the cell to acquire an active conformation. Thiol-disulphide oxidoreductases are enzymes that catalyse the formation of disulphide bonds. The bacterium Streptomyces lividans is a well-known host...
Main Authors: | Sonia Gullón, Silvia Marín, Rafael P. Mellado |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2019-07-01
|
Series: | Microbial Cell Factories |
Subjects: | |
Online Access: | http://link.springer.com/article/10.1186/s12934-019-1175-0 |
Similar Items
-
Thiol-disulphide homeostasis in essential thrombocythemia patients
by: Sentürk-Yikilmaz Aysun, et al.
Published: (2019-01-01) -
Dynamic thiol and disulphide homoeostasis in fibromyalgia
by: Gulsah Karatas, et al.
Published: (2019-08-01) -
The effect of hot-iron disbudding on thiol-disulphide homeostasis in calves
by: Hasan ERDOĞAN, et al.
Published: (2018-12-01) -
Evaluation of Dynamic Disulphide/Thiol Homeostasis in Silica Exposed Workers
by: Meşide Gündüzöz, et al.
Published: (2017-04-01) -
Thiol-disulphide homeostasis in noncomplicated chronic otitis media
by: Arife Sezgin, et al.
Published: (2019-06-01)