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Literature summary for 4.2.2.3 extracted from

  • Yamamoto, S.; Sahara, T.; Sato, D.; Kawasaki, K.; Ohgiya, S.; Inoue, A.; Ojima, T.
    Catalytically important amino-acid residues of abalone alginate lyase HdAly assessed by site-directed mutagenesis (2008), Enzyme Microb. Technol., 43, 396-402.
No PubMed abstract available
Search for more literature for 4.2.2.3

Cloned(Commentary)

Cloned (Comment) Organism
expressed in yeast and Escherichia coli as a His-tagged fusion protein Haliotis discus hannai

Protein Variants

Protein Variants Comment Organism
K162A mutant shows comparable activity to wild-type enzyme Haliotis discus hannai
K196A mutant shows comparable activity to wild-type enzyme Haliotis discus hannai
K95A mutant is completely inactive Haliotis discus hannai
R110A mutation causes 65% or more inactivation Haliotis discus hannai
R119A mutation causes 65% or more inactivation Haliotis discus hannai
R92A mutation causes 65% or more inactivation Haliotis discus hannai

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 SDS-PAGE Haliotis discus hannai

Organism

Organism UniProt Comment Textmining
Haliotis discus hannai
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Haliotis discus hannai

Synonyms

Synonyms Comment Organism
alginate lyase
-
 Haliotis discus hannai
HdAly
-
 Haliotis discus hannai

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Haliotis discus hannai
35
-
-
 Haliotis discus hannai

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Haliotis discus hannai
8
-
-
 Haliotis discus hannai