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Literature summary for 4.2.2.3 extracted from

  • Hamza, A.; Piao, Y.L.; Kim, M.S.; Choi, C.H.; Zhan, C.G.; Cho, H.
    Insight into the binding of the wild type and mutated alginate lyase (AlyVI) with its substrate: a computational and experimental study (2011), Biochim. Biophys. Acta, 1814, 1739-1747.
    View publication on PubMed
Search for more literature for 4.2.2.3

Cloned(Commentary)

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

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

Organism UniProt Comment Textmining
Vibrio sp.
-
 gene alyVI
-
Vibrio sp. QY105
-
 gene alyVI
-

Purification (Commentary)

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

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.
a

Synonyms

Synonyms Comment Organism
alginate lyase
-
 Vibrio sp.
AlyVI
-
 Vibrio sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Vibrio sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Vibrio sp.

General Information

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.