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Literature summary for 3.6.4.13 extracted from

  • Beran, R.K.; Pyle, A.M.
    Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase (2008), J. Biol. Chem., 283, 29929-29937.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.13

Activating Compound

Activating Compound Comment Organism Structure
nonstructural protein 4A i.e. NS4A, stimulates serine protease activity of NS3 protein, helicase domain enhances serine protease activity and vice versa Hepacivirus C

Cloned(Commentary)

Cloned (Comment) Organism
NS3-plus and NS3/4a-plus genes expressed in Escherichia coli, generation of NS3-4A expression product, pET15b and pet-SUMO vector Hepacivirus C

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information protease activities of NS3-4A variants analyzed, uncleaved NS3/4A polyprotein lacks protease and helicase activities Hepacivirus C

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Hepacivirus C

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Hepacivirus C multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
 viral genotype 1a, version H77
-

Purification (Commentary)

Purification (Comment) Organism
truncated and full-length complexes between nonstructural protein 3 (NS3) and nonstructural protein 4A (NS4), NS3-4A complex purifies as two separable proteins, gel filtration, SDS-PAGE Hepacivirus C

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 the nonstructural protein 4A (NS4A) stimulates NS3 serine protease activity, truncated and full-length complexes between nonstructural protein 3 (NS3) and nonstructural protein 4A (NS4) purified, serine protease activities analyzed, NS3 protease domain enhances the RNA binding, ATPase, and RNA unwinding activities of the C-terminal NS3 helicase domain, isolated protease domain is much less reactive than full-length NS3, NS3 protease activity is enhanced by the presence of the NS3 helicase domain, indicating that the two domains have evolved to become completely interdependent Hepacivirus C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities Hepacivirus C ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
nonstructural protein 3 ambiguous Hepacivirus C
NS3 ambiguous Hepacivirus C