Structural and biochemical analysis of a type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum

Kim, Hyun Sook; Kwak, Geun Hee; Lee, Kitaik; Jo, Chang Hwa; Hwang, Kwang Yeon; Kim, Hwa Young

doi:10.1016/j.abb.2014.07.009

Cited by 9 publications

(15 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Section: Archaeal Msr Enzymes Characterizedmentioning

confidence: 99%

“…An fRMSR enzyme is characterized from the thermophilic archaeon Thermoplasma acidophilum (Ta) [ 44 ]. TafRMSR is the only archaeal MSR enzyme to date that can use an NADPH > Trx > TrxR system to reduce MetO in vitro [ 44 ]. Similarly to other fRMSR enzymes, TafRMSR reduces the free form of Met- R -O, not the protein MetO or Met- S -O forms [ 44 ].…”

Section: Archaeal Msr Enzymes Characterizedmentioning

confidence: 99%

“…TafRMSR is the only archaeal MSR enzyme to date that can use an NADPH > Trx > TrxR system to reduce MetO in vitro [ 44 ]. Similarly to other fRMSR enzymes, TafRMSR reduces the free form of Met- R -O, not the protein MetO or Met- S -O forms [ 44 ]. TafRMSR has three cysteine residues (Cys15, Cys60 and Cys84).…”

Section: Archaeal Msr Enzymes Characterizedmentioning

confidence: 99%

“…TafRMSR has three cysteine residues (Cys15, Cys60 and Cys84). Of these, Cys60 and Cys84 are critical for MetO reductase activity, whereas, Cys15 is unimportant [ 44 ]. Cys84 forms the active site nucleophile (Cys A ) [ 44 ].…”

Section: Archaeal Msr Enzymes Characterizedmentioning

confidence: 99%

“…Of these, Cys60 and Cys84 are critical for MetO reductase activity, whereas, Cys15 is unimportant [ 44 ]. Cys84 forms the active site nucleophile (Cys A ) [ 44 ]. Cys60, while important for activity, does not form a disulfide bond with Cys84 and, thus, is not considered a resolving cysteine (Cys R ) [ 44 ].…”

Section: Archaeal Msr Enzymes Characterizedmentioning

confidence: 99%

See 4 more Smart Citations

Methionine Sulfoxide Reductases of Archaea

Maupin-Furlow

2018

Antioxidants

View full text Add to dashboard Cite

Methionine sulfoxide reductases are found in all domains of life and are important in reversing the oxidative damage of the free and protein forms of methionine, a sulfur containing amino acid particularly sensitive to reactive oxygen species (ROS). Archaea are microbes of a domain of life distinct from bacteria and eukaryotes. Archaea are well known for their ability to withstand harsh environmental conditions that range from habitats of high ROS, such as hypersaline lakes of intense ultraviolet (UV) radiation and desiccation, to hydrothermal vents of low concentrations of dissolved oxygen at high temperature. Recent evidence reveals the methionine sulfoxide reductases of archaea function not only in the reduction of methionine sulfoxide but also in the ubiquitin-like modification of protein targets during oxidative stress, an association that appears evolutionarily conserved in eukaryotes. Here is reviewed methionine sulfoxide reductases and their distribution and function in archaea.

show abstract

Section: Archaeal Msr Enzymes Characterizedmentioning

confidence: 99%