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Literature summary for 3.4.22.44 extracted from

  • Kim, D.H.; Hwang, D.C.; Kang, B.H.; Lew, J.; Han, J.S.; Song, B.O.D.; Choi, K.Y.
    Effects of internal cleavages and mutations in the C-terminal region of NIa protease of turnip mosaic potyvirus on the catalytic activity (1996), Virology, 226, 183-190.
    View publication on PubMed
Search for more literature for 3.4.22.44

Protein Variants

Protein Variants Comment Organism
G224R almost no self-cleavage of the 25 kDa protein turnip mosaic potyvirus
additional information comparison of the catalytic activities of wild-type, mutant and C-terminal truncated proteases turnip mosaic potyvirus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.22
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease turnip mosaic potyvirus
2.64
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 25 kDa protease turnip mosaic potyvirus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nuclear inclusion protein a + H2O turnip mosaic potyvirus the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein ?
-
 ?
nuclear inclusion protein a + H2O turnip mosaic potyvirus TuMV the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein ?
-
 ?

Organism

Organism UniProt Comment Textmining
turnip mosaic potyvirus
-
 TuMV
-
turnip mosaic potyvirus TuMV
-
 TuMV
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide + H2O
-
 turnip mosaic potyvirus ?
-
 ?
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide + H2O
-
 turnip mosaic potyvirus TuMV ?
-
 ?
nuclear inclusion protein a + H2O the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein turnip mosaic potyvirus ?
-
 ?
nuclear inclusion protein a + H2O the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein turnip mosaic potyvirus TuMV ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15
-
 temperature optimum for the 24 kDa protein turnip mosaic potyvirus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
15
-
 instable above turnip mosaic potyvirus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease turnip mosaic potyvirus
0.33
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 25 kDa protease turnip mosaic potyvirus