scholarly journals Neutral sphingomyelinase-2 is a redox sensitive enzyme: role of catalytic cysteine residues in regulation of enzymatic activity through changes in oligomeric state

2015 ◽  
Vol 465 (3) ◽  
pp. 371-382 ◽  
Author(s):  
P. Patrick Dotson ◽  
Alexander A. Karakashian ◽  
Mariana N. Nikolova-Karakashian
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Cysteine Residues ◽  
Oligomeric State ◽  
Neutral Sphingomyelinase ◽  
Catalytic Cysteine

Neutral sphingomyelinase-2 (nSMase-2) regulates cellular levels of ceramide. This manuscript shows that nSMase-2 is a redox-sensitive enzyme that oligomerizes via Cys617-mediated intermolecular bonds that is linked to suppressed enzyme activity, and may be a substrate for thioredoxin.

scholarly journals The role of cysteine residues in structure and enzyme activity of a maize β-glucosidase

1999 ◽  
Vol 266 (3) ◽  
pp. 1056-1065 ◽  
Author(s):  
Vladimír Rotrekl ◽  
Eliška Nejedlá ◽  
Igor Kučera ◽  
Fuad Abdallah ◽  
Klaus Palme ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cysteine Residues

Antiviral and Antiproliferative Activities of Interferon-α1: The Role of Cysteine Residues

1986 ◽  
Vol 6 (6) ◽  
pp. 677-685 ◽  
Author(s):  
MANFRED W. BEILHARZ ◽  
IAN T. NISBET ◽  
MARTIN J. TYMMS ◽  
PAUL J. HERTZOG ◽  
ANTHONY W. LINNANE
Keyword(s):  
Cysteine Residues ◽  
Antiproliferative Activities

scholarly journals Potential Dual Role of West Nile Virus NS2B in Orchestrating NS3 Enzymatic Activity in Viral Replication

Viruses ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 216
Author(s):  
Alanna C. Tseng ◽  
Vivek R. Nerurkar ◽  
Kabi R. Neupane ◽  
Helmut Kae ◽  
Pakieli H. Kaufusi
Keyword(s):  
West Nile Virus ◽  
Enzymatic Activity ◽  
Nonstructural Protein ◽  
Antiviral Drug ◽  
West Nile ◽  
Biochemical Assays ◽  
In Trans ◽  
Viral Polyprotein ◽  
Ns3 Protease

West Nile virus (WNV) nonstructural protein 3 (NS3) harbors the viral triphosphatase and helicase for viral RNA synthesis and, together with NS2B, constitutes the protease responsible for polyprotein processing. NS3 is a soluble protein, but it is localized to specialized compartments at the rough endoplasmic reticulum (RER), where its enzymatic functions are essential for virus replication. However, the mechanistic details behind the recruitment of NS3 from the cytoplasm to the RER have not yet been fully elucidated. In this study, we employed immunofluorescence and biochemical assays to demonstrate that NS3, when expressed individually and when cleaved from the viral polyprotein, is localized exclusively to the cytoplasm. Furthermore, NS3 appeared to be peripherally recruited to the RER and proteolytically active when NS2B was provided in trans. Thus, we provide evidence for a potential additional role for NS2B in not only serving as the cofactor for the NS3 protease, but also in recruiting NS3 from the cytoplasm to the RER for proper enzymatic activity. Results from our study suggest that targeting the interaction between NS2B and NS3 in disrupting the NS3 ER localization may be an attractive avenue for antiviral drug discovery.

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