Cloned (Comment) | Organism |
---|---|
gene alyVI, expression of GST-fusion wild-type and mutant enzymes in Escherichia coli strain BL-21 LysS | Vibrio sp. |
Protein Variants | Comment | Organism |
---|---|---|
D226G | site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme | Vibrio sp. |
H200A | site-directed mutagenesis, inactive mutant | Vibrio sp. |
K308A | site-directed mutagenesis, inactive mutant | Vibrio sp. |
L224V | site-directed mutagenesis, the mutant shows wild-type enzyme activity | Vibrio sp. |
L224V/D226G | site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme | Vibrio sp. |
additional information | detailed mutant analysis, overview | Vibrio sp. |
N138S | site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme | Vibrio sp. |
N217D | site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme | Vibrio sp. |
T136S | site-directed mutagenesis, the mutant shows wild-type enzyme activity | Vibrio sp. |
W165A | site-directed mutagenesis, inactive mutant | Vibrio sp. |
Y306F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Vibrio sp. |
Y312A | site-directed mutagenesis, inactive mutant | Vibrio sp. |
Y312F | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Vibrio sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio sp. | - |
gene alyVI | - |
Vibrio sp. QY105 | - |
gene alyVI | - |
Purification (Comment) | Organism |
---|---|
recombinant GST-fusion wild-type and mutant enzymes from Escherichia coli strain BL-21 LysS by glutathione affinity chromatography | Vibrio sp. |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1 | residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues, substrate binding mode, overview | Vibrio sp. |
Synonyms | Comment | Organism |
---|---|---|
alginate lyase | - |
Vibrio sp. |
AlyVI | - |
Vibrio sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Vibrio sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Vibrio sp. |
General Information | Comment | Organism |
---|---|---|
additional information | homology modeling using structure of family 7 alginate lyase from Sphingomonas sp. A1, structure-affinity relationships of aliginate lyase alyVI with its substrate, molecular docking, molecular dynamics simulations and binding free energy calculations, overview. Residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues | Vibrio sp. |