Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.22.46 extracted from

  • Kuehnel, E.; Cencic, R.; Foeger, N.; Skern, T.
    Foot-and-mouth disease virus leader proteinase: specificity at the P2 and P3 positions and comparison with other papain-like enzymes (2004), Biochemistry, 43, 11482-11490.
    View publication on PubMed
Search for more literature for 3.4.22.46

Cloned(Commentary)

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Foot-and-mouth disease virus
-
 FMDV
-
Foot-and-mouth disease virus FMDV
-
 FMDV
-

Posttranslational Modification

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 [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
Leader proteinase
-
 Foot-and-mouth disease virus
Lpro
-
 Foot-and-mouth disease virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Foot-and-mouth disease virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Foot-and-mouth disease virus