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Literature summary for 3.4.22.44 extracted from

  • Kim, D.H.; Hwang, D.C.; Kang, B.H.; Lew, J.; Choi, K.Y.
    Characterization of NIa protease from turnip mosaic potyvirus exhibiting a low-temperature optimum catalytic activity (1996), Virology, 221, 245-249.
    View publication on PubMed
Search for more literature for 3.4.22.44

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.51
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.0, 12°C turnip mosaic potyvirus
0.52
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.4, 12°C turnip mosaic potyvirus
0.62
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 8.0, 12°C turnip mosaic potyvirus
1.14
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.0, 25°C turnip mosaic potyvirus
1.2
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.4, 25°C turnip mosaic potyvirus
2.83
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 8.0, 25°C 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
-
 ?
-
 ?
nuclear inclusion protein a + H2O turnip mosaic potyvirus TuMV
-
 ?
-
 ?

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
-
 turnip mosaic potyvirus ?
-
 ?
nuclear inclusion protein a + H2O
-
 turnip mosaic potyvirus TuMV ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15
-
 temperature optimum of the 27 kDa full length protease. The optimum is not related to the C-terminal cleavage site but to the stability or flexibility of the structure of the NIa protease turnip mosaic potyvirus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.12
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.0, 12°C turnip mosaic potyvirus
0.19
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.0, 25°C turnip mosaic potyvirus
0.22
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.4, 12°C turnip mosaic potyvirus
0.34
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 7.4, 25°C turnip mosaic potyvirus
0.373
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 8.0, 12°C turnip mosaic potyvirus
1.01
-
 acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide 27 kDa full length protease, pH 8.0, 25°C turnip mosaic potyvirus