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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Reaction: 3.4.21.114

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions

EC Number: 3.4.21.114

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: equine arterivirus serine peptidase

Summary:
The reaction is defined as the cleavage of (Glu/Gln)|(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab (ORF1ab is shown in this reaction).

In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins. This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12). It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position. Cleavage of ORF1ab by this enzyme is essential for viral replication. Belongs to peptidase family S32.

Enzyme Commission Summary:
The reaction is defined as the cleavage of (Glu/Gln)|(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab (ORF1a is shown in this reaction).

In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins. This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12). It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position. Cleavage of ORF1ab by this enzyme is essential for viral replication. Belongs to peptidase family S32.

Citations: [BarretteNg02, vanDinten99, Snijder96]

Relationship Links: BRENDA:EC:3.4.21.114 , ENZYME:EC:3.4.21.114 , IUBMB-ExplorEnz:EC:3.4.21.114


References

BarretteNg02: Barrette-Ng IH, Ng KK, Mark BL, Van Aken D, Cherney MM, Garen C, Kolodenko Y, Gorbalenya AE, Snijder EJ, James MN (2002). "Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole." J Biol Chem 277(42);39960-6. PMID: 12163505

Snijder96: Snijder EJ, Wassenaar AL, van Dinten LC, Spaan WJ, Gorbalenya AE (1996). "The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases." J Biol Chem 271(9);4864-71. PMID: 8617757

vanDinten99: van Dinten LC, Rensen S, Gorbalenya AE, Snijder EJ (1999). "Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and Is essential for virus replication." J Virol 73(3);2027-37. PMID: 9971783


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC13A.