Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes by in vitro transcription and translation using rabbit reticulocyte lysate | Foot-and-mouth disease virus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | mutation of the viral polyprotein self-processing cleavage site QRKLK*GAGQ, replacement by several variants of the two protein substrate elIF4G cleavage sites ANLG*RTTL and LNVG*SRRS, overview | Foot-and-mouth disease virus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
eukaryotic initiation factor eIF4GI + H2O | Foot-and-mouth disease virus | eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL | ? | - |
? | |
eukaryotic initiation factor eIF4GI + H2O | Foot-and-mouth disease virus FMDV | eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL | ? | - |
? | |
eukaryotic initiation factor eIF4GII + H2O | Foot-and-mouth disease virus | eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP | ? | - |
? | |
eukaryotic initiation factor eIF4GII + H2O | Foot-and-mouth disease virus FMDV | eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Foot-and-mouth disease virus | - |
FMDV | - |
Foot-and-mouth disease virus FMDV | - |
FMDV | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the enzyme is synthesized as part of a large polyprotein LbproVP4VP2, from which it releases itself by highly efficient self-processing between its C- and N-terminus of the subsequent protein VP4, recognition of the sequence QRKLK*GAGQ, Asp at P3 and Phe at P2 severely compromise the self-processing | Foot-and-mouth disease virus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
self-processing activity of the enzyme on wild-type and mutant polyproteins, overview | Foot-and-mouth disease virus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
eukaryotic initiation factor eIF4GI + H2O | eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL | Foot-and-mouth disease virus | ? | - |
? | |
eukaryotic initiation factor eIF4GI + H2O | eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL | Foot-and-mouth disease virus FMDV | ? | - |
? | |
eukaryotic initiation factor eIF4GII + H2O | eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP | Foot-and-mouth disease virus | ? | - |
? | |
eukaryotic initiation factor eIF4GII + H2O | eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP | Foot-and-mouth disease virus FMDV | ? | - |
? | |
additional information | the enzyme is synthesized as part of a large polyprotein LbproVP4VP, from which it releases itself by highly efficient self-processing between its C- and N-terminus of the subsequent protein VP4, recognition of the sequence QRKLK*GAGQ, specificity at the P2, Leu, and P3 positions, including S3 subsite preferring Lys or Asn, and comparison with other papain-like enzymes, no activity when Pro is at P2 position and with type I collagen, overview, residues P99, P100, L143, A149, and L178 determine the specificity of the S2 binding pocket | Foot-and-mouth disease virus | ? | - |
? | |
additional information | the enzyme is synthesized as part of a large polyprotein LbproVP4VP, from which it releases itself by highly efficient self-processing between its C- and N-terminus of the subsequent protein VP4, recognition of the sequence QRKLK*GAGQ, specificity at the P2, Leu, and P3 positions, including S3 subsite preferring Lys or Asn, and comparison with other papain-like enzymes, no activity when Pro is at P2 position and with type I collagen, overview, residues P99, P100, L143, A149, and L178 determine the specificity of the S2 binding pocket | Foot-and-mouth disease virus FMDV | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Leader proteinase | - |
Foot-and-mouth disease virus |
Lpro | - |
Foot-and-mouth disease virus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Foot-and-mouth disease virus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Foot-and-mouth disease virus |