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Literature summary extracted from

  • Sommergruber, W.; Ahorn, H.; Z๖phel, A.; Maurer-Fogy, I.; Fessl, F.; Schnorrenberg, G.; Liebig, H.D.; Blaas, D.; Kuechler, E.; Skern, T.
    Cleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A (1992), J. Biol. Chem., 267, 22639-22644.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.29 human rhinovirus type 2 Human rhinovirus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.29 1,10-phenanthroline
-
Human rhinovirus sp.
3.4.22.29 3,4-dichloroisocoumarin
-
Human rhinovirus sp.
3.4.22.29 antipain eIF-4gamma as substrate in HeLa cell extracts; human rhinovirus Human rhinovirus sp.
3.4.22.29 Ca2+ 50 mM, weak Human rhinovirus sp.
3.4.22.29 chymostatin eIF-4gamma as substrate in HeLa cell extracts; human rhinovirus Human rhinovirus sp.
3.4.22.29 Co2+ 0.05 mM Human rhinovirus sp.
3.4.22.29 Cu2+ 0.05 mM Human rhinovirus sp.
3.4.22.29 EDTA at high concentration Human rhinovirus sp.
3.4.22.29 Elastinal eIF-4gamma as substrate in HeLa cell extracts; human rhinovirus Human rhinovirus sp.
3.4.22.29 Hg2+ 0.05 mM Human rhinovirus sp.
3.4.22.29 iodoacetamide strong Human rhinovirus sp.
3.4.22.29 leupeptin not Human rhinovirus sp.
3.4.22.29 Mg2+ 50 mM, weak Human rhinovirus sp.
3.4.22.29 Mn2+ 2 mM; weak Human rhinovirus sp.
3.4.22.29 additional information no inhibition by amastatin, bestatin, epiamastatin, foroxymithin, phosphoramidon, Nle-statine-Ala-statine and APMSF; no inhibition by trans-epoxysuccinyl-L-leucylamido(4-guanidino)-butane (i.e. E-64) Human rhinovirus sp.
3.4.22.29 NEM strong Human rhinovirus sp.
3.4.22.29 tosyl-L-leucine-chloromethyl ketone
-
Human rhinovirus sp.
3.4.22.29 tosyl-L-phenylalanine-chloromethyl ketone weak Human rhinovirus sp.
3.4.22.29 Zn2+ 0.05 mM Human rhinovirus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.22.29 NaCl activation, 0.15-1.25 M Human rhinovirus sp.

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.29 Human rhinovirus sp.
-
serotypes 2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.29 partial Human rhinovirus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.29 Arg-Arg-Asn-Thr-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O peptide derived from poliovirus type 1 polyprotein, poor substrate Human rhinovirus sp. Arg-Arg-Asn-Thr-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O i.e. synthetic peptide P7-P8', hydrolyzed with about the same relative efficiency compared to P8-P8' Human rhinovirus sp. Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Glu-Arg-Ala-Ser-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O peptide derived from poliovirus type 1 polyprotein Human rhinovirus sp. Glu-Arg-Ala-Ser-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O i.e. synthetic peptide P5-P8', poor substrate Human rhinovirus sp. Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O i.e. synthetic peptide P4-P8', poor substrate Human rhinovirus sp. Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 modified pentadecameric peptides + H2O i.e. synthetic P8-P7' peptides, intermolecular specificity, changes at P2 and P1' are highly deleterious Human rhinovirus sp. ?
-
?
3.4.22.29 additional information no hydrolysis of some modified pentadecameric synthetic peptides P8-P7'(overview), synthetic peptides P3-P8', Arg-Lys-Gly-Asp-Ile-Lys-Ser-Tyr-Gly-Ile-Gly-Pro-Arg-Tyr-Gly-Gly, Asn-Val-Arg-Ala-Val-Lys-Asn-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His, Asp-Val-Phe-Thr-Asn-Val-Gly-Pro-Ser-Ser-Met-Phe-Val-His Human rhinovirus sp. ?
-
?
3.4.22.29 additional information synthetic peptides with replacements of P1 or P1' residues with epsilon-amino caproic acid or statine Human rhinovirus sp. ?
-
?
3.4.22.29 Pro-Arg-Ala-Ser-Met-Lys-Thr-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O poor substrate Human rhinovirus sp. Pro-Arg-Ala-Ser-Met-Lys-Thr-Val + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Pro-Arg-Glu-Asn-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O peptide derived from poliovirus type 1 polyprotein, poor substrate Human rhinovirus sp. Pro-Arg-Glu-Asn-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met + H2O i.e. synthetic peptide P6-P5', hydrolyzed with 42% relative efficiency compared to P8-P8' Human rhinovirus sp. Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met
-
?
3.4.22.29 Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr + H2O i.e. synthetic peptide P6-P6', hydrolyzed with 45% relative efficiency compared to P8-P8', smallest cleavable symmetric peptide Human rhinovirus sp. Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr
-
?
3.4.22.29 Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val + H2O i.e. synthetic peptide P6-P7', hydrolyzed with 55% relative efficiency compared to P8-P8' Human rhinovirus sp. Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val
-
?
3.4.22.29 Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O i.e. synthetic peptide P6-P8' Human rhinovirus sp. Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O hydrolyzed with 70% relative efficiency compared to P8-P8' Human rhinovirus sp. Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Ser-Arg-Ala-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O peptide derived from poliovirus type 1 polyprotein Human rhinovirus sp. Ser-Arg-Ala-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?
3.4.22.29 Ser-Thr-Lys-Asp-Ile-Thr-Thr-Tyr-Gly-Phe-Gly-His-Gln-Asn-Lys-Ala + H2O poor substrate Human rhinovirus sp. Ser-Thr-Lys-Asp-Ile-Thr-Thr-Tyr + Glys-Phe-Gly-His-Gln-Asn-Lys-Ala
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly + H2O i.e. synthetic peptide P8-P1', poor substrate, smallest cleavable asymmetric peptide Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + glycine
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro + H2O i.e. synthetic peptide P8-P2', hydrolyzed with about the same relative efficiency as P8-P8' Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp + H2O i.e. peptide P8-P4' Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met + H2O i.e. peptide P8-P5' Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr + H2O i.e. synthetic peptide P8-6' Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val + H2O i.e. synthetic peptide P8-7' Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val
-
?
3.4.22.29 Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O i.e. synthetic peptide P8-P8' Human rhinovirus sp. Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.22.29 7 8.5 broad, synthetic peptide P8-P8' as substrate Human rhinovirus sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.22.29 6 9.2 about half-maximal activity at pH 6 and 9.2, synthetic peptide P8-P8' as substrate Human rhinovirus sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.22.29 4 9 20 min, room temperature, stable in this range, 50% loss of activity at pH 3 and 10.2 Human rhinovirus sp.