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Literature summary for 4.2.2.3 extracted from

  • Rahman, M.M.; Inoue, A.; Tanaka, H.; Ojima, T.
    cDNA cloning of an alginate lyase from a marine gastropod Aplysia kurodai and assessment of catalytically important residues of this enzyme (2011), Biochimie, 93, 1720-1730.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
AkAly30 DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3) Aplysia kurodai

Protein Variants

Protein Variants Comment Organism
K99A site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme Aplysia kurodai
N120H site-directed mutagenesis, reverse replacement of N120 by His in recAkAly30 increases the activity at pH 10.0 from 8 U/mg to 93 U/mg. However, the activity level at pH 7.0, i.e., 774.8 U/mg, is still much higher than that at pH 10.0 Aplysia kurodai
R128A site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme Aplysia kurodai
S126A site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme Aplysia kurodai
Y140F site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme Aplysia kurodai
Y142F site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme Aplysia kurodai

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29722
-
x * 29722, sequence calculation, x * 30000, SDS-PAGE Aplysia kurodai
30000
-
x * 29722, sequence calculation, x * 30000, SDS-PAGE Aplysia kurodai

Organism

Organism UniProt Comment Textmining
Aplysia kurodai E7FLQ2
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged AkAly30 33fold from Escherihcia coli strain BL21(DE3) by nickel affinity chromatography, native AkAly30 97.58fold by ammonium sulfate fractionation and cation exchange chromatography Aplysia kurodai

Source Tissue

Source Tissue Comment Organism Textmining
digestive juice
-
Aplysia kurodai
-
hepatopancreas
-
Aplysia kurodai
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2100
-
purified recombinant His-tagged AkAly30, pH 8.0, 30°C Aplysia kurodai
5796
-
purified native AkAly30, pH 8.0, 30°C Aplysia kurodai

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate is sodium alginate originating from Macrocystis pyrifera, preparation of poly(M)-rich, poly(G)-rich, and random substrates thereof Aplysia kurodai ?
-
?

Subunits

Subunits Comment Organism
? x * 29722, sequence calculation, x * 30000, SDS-PAGE Aplysia kurodai

Synonyms

Synonyms Comment Organism
AkAly30
-
Aplysia kurodai
alginate lyase
-
Aplysia kurodai
More the enzyme belongs to the polysaccharide-lyase-family 14, PL-14 Aplysia kurodai

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Aplysia kurodai

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Aplysia kurodai

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
residue N120 is not directly related to the pH-dependence of AkAly30, overview Aplysia kurodai

General Information

General Information Comment Organism
evolution the enzyme belongs to the polysaccharide-lyase-family 14, PL-14, primary structure analysis Aplysia kurodai
physiological function herbivorous marine gastropods such as abalone and sea hare ingest brown algae as a major diet and degrade the dietary alginate with alginate lyase in their digestive fluid Aplysia kurodai