Cloned (Comment) | Organism |
---|---|
gene bglA13, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli | Neocallimastix patriciarum |
gene bglA16, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli | Neocallimastix patriciarum |
gene bglA51, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli | Neocallimastix patriciarum |
gene bglM2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli | Neocallimastix patriciarum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | 0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum | |
additional information | - |
additional information | 0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum | |
additional information | - |
additional information | 0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum | |
additional information | - |
additional information | 1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neocallimastix patriciarum | I3W8N0 | BglM2; isolated from the feces of water buffalo, gene bglM2 | - |
Neocallimastix patriciarum | I3W8N1 | BglA51; isolated from the feces of water buffalo, gene bglA51 | - |
Neocallimastix patriciarum | I3W8N2 | BglA13; isolated from the feces of water buffalo, gene bglA13 | - |
Neocallimastix patriciarum | I3W8N3 | BglA16; isolated from the feces of water buffalo, gene bglA16 | - |
Neocallimastix patriciarum J11 | I3W8N0 | BglM2; isolated from the feces of water buffalo, gene bglM2 | - |
Neocallimastix patriciarum J11 | I3W8N1 | BglA51; isolated from the feces of water buffalo, gene bglA51 | - |
Neocallimastix patriciarum J11 | I3W8N2 | BglA13; isolated from the feces of water buffalo, gene bglA13 | - |
Neocallimastix patriciarum J11 | I3W8N3 | BglA16; isolated from the feces of water buffalo, gene bglA16 | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli | Neocallimastix patriciarum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
26530 | - |
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan | Neocallimastix patriciarum |
32100 | - |
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan | Neocallimastix patriciarum |
39520 | - |
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan | Neocallimastix patriciarum |
41210 | - |
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan | Neocallimastix patriciarum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
barley beta-glucan + H2O | best substrate | Neocallimastix patriciarum | ? | - |
? | |
barley beta-glucan + H2O | best substrate | Neocallimastix patriciarum J11 | ? | - |
? | |
lichenan + H2O | - |
Neocallimastix patriciarum | ? | - |
? | |
lichenan + H2O | - |
Neocallimastix patriciarum J11 | ? | - |
? | |
additional information | no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan | Neocallimastix patriciarum | ? | - |
? | |
additional information | no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan | Neocallimastix patriciarum J11 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
beta-1,3-1,4-glucanase | - |
Neocallimastix patriciarum |
BglA13 | - |
Neocallimastix patriciarum |
BglA16 | - |
Neocallimastix patriciarum |
BglA51 | - |
Neocallimastix patriciarum |
BglM2 | - |
Neocallimastix patriciarum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
- |
Neocallimastix patriciarum |
50 | - |
- |
Neocallimastix patriciarum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
63.06 | - |
Barley beta-glucan | recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum | |
68.19 | - |
Barley beta-glucan | recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum | |
83.89 | - |
Barley beta-glucan | recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum | |
133.3 | - |
Barley beta-glucan | recombinant enzyme, pH 6.0, 40°C | Neocallimastix patriciarum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
- |
Neocallimastix patriciarum |
6.5 | - |
- |
Neocallimastix patriciarum |
General Information | Comment | Organism |
---|---|---|
evolution | the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11 | Neocallimastix patriciarum |