Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys …

J Choi, S Choi, J Choi, MK Cha, IH Kim… - Journal of Biological …, 2003 - ASBMB
Thioredoxin-dependent thiol peroxidase (Tpx) from Escherichia coli represents a group of
antioxidant enzymes that are widely distributed in pathogenic bacterial species and which
belong to the peroxiredoxin (Prx) family. Bacterial Tpxs are unique in that the location of the
resolving cysteine (CR) is different from those of other Prxs. E. coli Tpx (EcTpx) shows
substrate specificity toward alkyl hydroperoxides over H 2 O 2 and is the most potent
reductant of alkyl hydroperoxides surpassing AhpC and BCP, the other E. coli Prx members …

Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State

S Whanchul - Proceedings of the Korea Crystallographic …, 2003 - koreascience.kr
Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State -Proceedings of
the Korea Crystallographic Association Conference | Korea Science … Proceedings of the
Korea Crystallographic Association Conference (한국결정학회:학술대회논문집) … Crystal
Structure of Escherichia coli Thiol Peroxidase in the Oxidized State
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