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3.4.22.46: L-peptidase

This is an abbreviated version!
For detailed information about L-peptidase, go to the full flat file.

Word Map on EC 3.4.22.46

Reaction

autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-/-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-/-Arg- and -Lys-/-Arg- =

Synonyms

3C protease, 3Cpro, Eukaryotic signal peptidase, Eukaryotic signal proteinase, FMDV 3Cpro, foot-and-mouth disease virus 3C protease, L protein, L proteinase, Lab protein, Lb proC, Lbpro, Leader peptidase, leader peptidase B, leader peptidase NisP, Leader peptide hydrolase, leader protease, Leader proteinase, leaderprotease L1, leaderprotease L2, LepB, Lpro, nisin leader peptidase, NisP, nsp1alpha, P1a protein, Peptidase, signal, Prokaryotic leader peptidase, Prokaryotic signal peptidase, Prokaryotic signal proteinase, Propeptidase, Proteinase, eukaryotic signal, Proteinase, signal, Signal peptidase, Signalase, sLbpro

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.46 L-peptidase

Subunits

Subunits on EC 3.4.22.46 - L-peptidase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
dimer in solution, determined by NMR-spectroscopy. Dimer can not be dissociated by increasing the ionic strength or by dilution
homodimer
additional information
-
the peptide binding cleft, which contains the active site at its centre, is located at the interface between two beta-barrels. Unusually, picornaviral 3Cpro possess a Cys-His-Asp/Glu catalytic triad at the centre of this cleft, instead of the Ser-His-Asp arrangement of active-site residues