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Literature summary for 3.4.21.91 extracted from

  • Gruba, N.; Rodriguez Martinez, J.I.; Grzywa, R.; Wysocka, M.; Skorenski, M.; Burmistrz, M.; Lecka, M.; Lesner, A.; Sienczyk, M.; Pyrc, K.
    Substrate profiling of Zika virus NS2B-NS3 protease (2016), FEBS Lett., 590, 3459-3468 .
    View publication on PubMed
Search for more literature for 3.4.21.91

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of an active NS3pro domain fused with the NS2B cofactor (NS2BLNNS3pro) in a prokaryotic expression system Zika virus

Inhibitors

Inhibitors Comment Organism Structure
additional information screening for potential intracellular substrates of NS3 and development of specific inhibitors of ZIKV protease, overview Zika virus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.111
-
 N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide pH 7.4, 37°C, phosphate buffer Zika virus
0.444
-
 N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide pH 8.5, 37°C, Tris-CHAPS-glycerol buffer Zika virus

Organism

Organism UniProt Comment Textmining
Zika virus Q32ZE1 ZIKV, isolated from macaques in Uganda in 1947
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information screening for potential intracellular substrates of NS3, substrate specificity analysis of recombinant enzyme NS2BLNNS3pr using synthesized FRET-type substrate libraries, peptide library preparation. Profiling of the P1-P4 substrate specificity of the NS2B-NS3 protease using a combinatorial chemistry approach and the split-and-mix method. Arg is the only preferred P1 residue of the enzyme, preference for Val at P4, and Lys at P3 and P2, no activity for Trp, Tyr, Asp, and Pro at P3 position, structure-function analysis, overview Zika virus ?
-
 ?
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide + H2O substrate binding structure in the enzyme's active site (PDB ID 5LC0), modeling. The peptidic substrate with the sequence ABZ-Val-Lys-Lys-Arg-ANB-NH2 is selected as the most efficient peptidic substrate with the nonprimed binding sites of ZIKV NS3 protease Zika virus N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-L-arginine + 5-amino-2-nitrobenzamide
-
 ir
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
-
 Zika virus Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
 ?

Synonyms

Synonyms Comment Organism
NS2B-NS3 protease
-
 Zika virus
NS2B-NS3 serine protease
-
 Zika virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Zika virus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
25.94
-
 N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide pH 7.4, 37°C, phosphate buffer Zika virus
343.73
-
 N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide pH 8.5, 37°C, Tris-CHAPS-glycerol buffer Zika virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4 8.5 assay at Zika virus

Cofactor

Cofactor Comment Organism Structure
NS2B cofactor protein essential for activity Zika virus

General Information

General Information Comment Organism
evolution comparative analysis of the substrate specificity reveals that ZIKV NS3 protease follows the typical pattern for flaviviruses Zika virus
physiological function ZIKV expresses the serine protease NS3 which is responsible for viral protein processing and replication Zika virus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
235
-
 N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide pH 7.4, 37°C, phosphate buffer Zika virus
7760
-
 N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide pH 8.5, 37°C, Tris-CHAPS-glycerol buffer Zika virus