Peptide name : D (KLAKLAK) 2-TAT

Source/Organism : Not found

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 25

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : IC50 : 5.3 μM

Cell line : A549

Cancer type : Not specified

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2959.6817 Dalton

Aliphatic index : 0.784

Instability index : 87.036

Hydrophobicity (GRAVY) : -1.604

Isoelectric point : 12

Charge (pH 7) : 13.752

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 0.66666666

hydrophobic moment : 0.0587

Missing amino acid : C,W,H,T,P,M,I,E,F,S,D,Y,N,V

Most occurring amino acid : K

Most occurring amino acid frequency : 8

Least occurring amino acid : Q

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.6, 0.0, 0.1)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O

1 : Zhang D, et al. Cloning and characterization of a novel mesophilic xylanase gene Fgxyn3 from Fusarium graminearum Z-1. 3 Biotech. 2024; 14:162. doi: 10.1007/s13205-024-03973-0

Paper title : Cloning and characterization of a novel mesophilic xylanase gene Fgxyn3 from Fusarium graminearum Z-1.

Doi : https://doi.org/10.1007/s13205-024-03973-0

Abstract : UNLABELLED: In order to search for high specific activity and the resistant xylanases to XIP-I and provide more alternative xylanases for industrial production, a strain of Fusarium graminearum from Triticum aestivum grains infected with filamentous fungus produced xylanases was isolated and identified. Three xylanase genes from Fusarium graminearum Z-1 were cloned and successfully expressed in E. coli and P. pastoris, respectively. The specific activities of Fgxyn1, _EFgxyn2 and _EFgxyn3 for birchwood xylan were 38.79, 0.85 and 243.83 U/mg in E. coli, and 40.11, 0 and 910.37 U/mg in P. pastoris, respectively. _EFgxyn3 and _PFgxyn3 had the similar optimum pH at 6.0 and pH stability at 5.0-9.0. However, they had different optimum temperature and thermal stability, with 30 °C for _EFgxyn3 and 40 °C for _PFgxyn3, and 4-35 °C for _EFgxyn3 and 4-40 °C for _PFgxyn3, respectively. The substrate spectrum and the kinetic parameters showed that the two xylanases also exhibited the highest xylanase activity and catalytic efficiency (k_cat/k_m) toward birchwood xylan, with 243.83 U/mg and 61.44 mL/mg/s for _EFgxyn3 and 910.37 U/mg and 910.37 mL/mg/s for _PFgxyn3, respectively. This study provided a novel mesophilic xylanase with high specific activity and catalytic efficiency, thus making it a promising candidate for extensive applications in animal feed and food industry. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13205-024-03973-0.