Literature summary for 3.4.22.29 extracted from

Sommergruber, W.; Seipelt, J.; Fessl, F.; Skern, T.; Liebig, H.D.; Casari, G.
Mutational analyses support a model for the HRV2 2A proteinase (1997), Virology, 234, 203-214.

Search for more literature for 3.4.22.29

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Human rhinovirus sp.

Protein Variants

Protein Variants	Comment	Organism
134Rstop	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
C101S	intramolecular cleavage is reduced to 52% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 20% of that of the wild-type enzyme, cleavage of eIF4G is 75-100% of that of the wild-type enzyme	Human rhinovirus sp.
C106S	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
C112S	intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G	Human rhinovirus sp.
C138A	intramolecular cleavage is reduced to 90% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 200% of that of the wild-type enzyme, cleavage of eIF4G is 75-100% of that of the wild-type enzyme	Human rhinovirus sp.
C52A	intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G	Human rhinovirus sp.
C54A	intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G	Human rhinovirus sp.
C61A	intramolecular cleavage is reduced to 54% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 40% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme	Human rhinovirus sp.
D105N	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
D105T	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
D132R/R134D	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
D132T	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
D35A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
D35E	intramolecular cleavage is reduced to 16% of the wild-type activity, cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
D35T	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
DELTAG104	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
DELTAG107/108	cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
F130L	intramolecular cleavage is completely abolished	Human rhinovirus sp.
F130S	intramolecular cleavage is completely abolished	Human rhinovirus sp.
F130V	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
F136V	intramolecular cleavage is reduced to 57% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 25% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme	Human rhinovirus sp.
G115A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
G115S	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
G118A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
G118S	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
G123A	intramolecular cleavage is reduced to 23% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 8% of that of the wild-type enzyme, cleavage of eIF4G is less than 10% of that of the wild-type enzyme	Human rhinovirus sp.
G123A/G124A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
G123S	intramolecular cleavage is reduced to 20% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 10% of that of the wild-type enzyme, cleavage of eIF4G is below 10% of that of the wild-type enzyme	Human rhinovirus sp.
G124A	intramolecular cleavage is reduced to 22% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 9% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme	Human rhinovirus sp.
G124S	intramolecular cleavage is reduced to 30% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 10% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme	Human rhinovirus sp.
H114G	intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G	Human rhinovirus sp.
H114N	mutant enzyme does not contain Zn2+	Human rhinovirus sp.
H114N	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
H135stop	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
H18A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
H18Y	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
K113P/H114A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
L19S	cleavage of P8-P8' is reduced to 42% of the wild-type activity	Human rhinovirus sp.
L19S	intramolecular cleavage activity is reduced to 80% of that of the wild-type activity, cleavage of P8-P8' is reduced to 42% of the wild-type activity	Human rhinovirus sp.
additional information	the presence of an extensive C-terminal helix, in which Asp132, Arg134, Phe130 and Phe136 play important roles, explains why mutations in this region are generally detrimental to proteinase activity.The zinc-binding motif comprises Cys52, Cys54, Cys112 and His114. Exchange of these residues inactivates the enzyme	Human rhinovirus sp.
N16A	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
R134Q	intramolecular cleavage and cleavage of P8-P8' is completely abolished, no cleavage of eIF4G is detected	Human rhinovirus sp.
T121Y	intramolecular cleavage and cleavage of P8-P8' is completely abolished	Human rhinovirus sp.
Y85K	intramolecular cleavage is reduced to 82% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 39% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme	Human rhinovirus sp.
Y85T	intramolecular cleavage is reduced to 74% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 32% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme	Human rhinovirus sp.
Y85T	intramolecular cleavage is reduced to 27% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 8% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme	Human rhinovirus sp.
Y86F	intramolecular cleavage is reduced to 62% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 21% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme	Human rhinovirus sp.
Y86K	intramolecular cleavage is reduced to 71% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 34% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme	Human rhinovirus sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the enzyme contains a tightly bound Zn2+ required for structural integrity	Human rhinovirus sp.
Zn2+	the zinc-binding motif comprises Cys52, Cys54, Cys112 and His114	Human rhinovirus sp.

Organism

Organism	UniProt	Comment	Textmining
Human rhinovirus sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
eIF4G + H2O	-	Human rhinovirus sp.	?	-	?
additional information	residues Gly123, Gly124, Thr121 and Cys101 are proposed to be involved in the architecture of the substrate binding pocket and to provide the correct environment for the catalytic triad of His18, Asp35, and Cys106. Residues Tyr85 and Tyr86 are thought to participate in substrate recognition	Human rhinovirus sp.	?	-	?
TRPIITTAGPSDMYV + H2O	-	Human rhinovirus sp.	TRPIITTA + GPSDMYV	-	?