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 | 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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Aplysia kurodai | E7FLQ2 | - |
- |
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 | Comment | Organism | Textmining |
---|---|---|---|
digestive juice | - |
Aplysia kurodai | - |
hepatopancreas | - |
Aplysia kurodai | - |
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 | 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 | Comment | Organism |
---|---|---|
? | x * 29722, sequence calculation, x * 30000, SDS-PAGE | Aplysia kurodai |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Aplysia kurodai |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Aplysia kurodai |
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 | 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 |