Type | Description |
---|---|
Definition | peroxiredoxin |
Date | Results | Publications |
---|---|---|
2015-04-25 12:26:00 | Using bulkier hydroperoxide substrates with higher Km values, ths study found that different efficiencies (kcat/Km) for turnover of AhpC with these substrates are primarily caused by their slower rates of binding. | 25633283 |
2010-01-21 00:00:00 | findings support the modular architecture of AhpF and its need for domain rotations for function, and emphasize the importance of Cys165 in the reductive reactivation of AhpC. | 17441733 |
2010-01-21 00:00:00 | The connection is clarified between peroxiredoxin (Prx) AhpC decamer formation and active site loop dynamics and the impact of their disruption on both catalytic activity and susceptibility of Prxs to inactivation during turnover | 16060667 |
2010-01-21 00:00:00 | Salmonella typhimurium alkyl hydroperoxide reductase C component substrate specificity profile and redox potential were studied. | 18165315 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
AHPC_SALTY
UniprotKB:
P0A251
UniParc:
UPI000002FC85
EMBL:
AE006468,
J05478
EnsemblGenome:
STM0608
KO:
stm:STM0608
|
Nucleutide sequences |
EMBL-CDS:
AAL19559.1,
AAA16431.1
EnsemblGenome_TRS:
AAL19559
|
Protein sequencees |
EnsemblGenome_PRO:
AAL19559
RefSeq:
NP_459600.1
|
Others |
UniRef100:
UniRef100_P0A252
UniRef90:
UniRef90_P0AE10
UniRef50:
UniRef50_P0AE10
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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