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Literature summary extracted from

  • Hung, Y.L.; Chen, H.J.; Liu, J.C.; Chen, Y.C.
    Catalytic efficiency diversification of duplicate beta-1,3-1,4-glucanases from Neocallimastix patriciarum J11 (2012), Appl. Environ. Microbiol., 78, 4294-4300.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 gene bglA13, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli Neocallimastix patriciarum
3.2.1.73 gene bglA16, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli Neocallimastix patriciarum
3.2.1.73 gene bglA51, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli Neocallimastix patriciarum
3.2.1.73 gene bglM2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli Neocallimastix patriciarum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 additional information
-
 additional information 0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum
3.2.1.73 additional information
-
 additional information 0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum
3.2.1.73 additional information
-
 additional information 0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum
3.2.1.73 additional information
-
 additional information 1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Neocallimastix patriciarum I3W8N0 BglM2; isolated from the feces of water buffalo, gene bglM2
-
3.2.1.73 Neocallimastix patriciarum I3W8N1 BglA51; isolated from the feces of water buffalo, gene bglA51
-
3.2.1.73 Neocallimastix patriciarum I3W8N2 BglA13; isolated from the feces of water buffalo, gene bglA13
-
3.2.1.73 Neocallimastix patriciarum I3W8N3 BglA16; isolated from the feces of water buffalo, gene bglA16
-
3.2.1.73 Neocallimastix patriciarum J11 I3W8N0 BglM2; isolated from the feces of water buffalo, gene bglM2
-
3.2.1.73 Neocallimastix patriciarum J11 I3W8N1 BglA51; isolated from the feces of water buffalo, gene bglA51
-
3.2.1.73 Neocallimastix patriciarum J11 I3W8N2 BglA13; isolated from the feces of water buffalo, gene bglA13
-
3.2.1.73 Neocallimastix patriciarum J11 I3W8N3 BglA16; isolated from the feces of water buffalo, gene bglA16
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.73 recombinant enzyme from Escherichia coli Neocallimastix patriciarum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.73 26530
-
 purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan Neocallimastix patriciarum
3.2.1.73 32100
-
 purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan Neocallimastix patriciarum
3.2.1.73 39520
-
 purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan Neocallimastix patriciarum
3.2.1.73 41210
-
 purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan Neocallimastix patriciarum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 barley beta-glucan + H2O best substrate Neocallimastix patriciarum ?
-
 ?
3.2.1.73 barley beta-glucan + H2O best substrate Neocallimastix patriciarum J11 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Neocallimastix patriciarum ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Neocallimastix patriciarum J11 ?
-
 ?
3.2.1.73 additional information no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan Neocallimastix patriciarum ?
-
 ?
3.2.1.73 additional information no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan Neocallimastix patriciarum J11 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 beta-1,3-1,4-glucanase
-
 Neocallimastix patriciarum
3.2.1.73 BglA13
-
 Neocallimastix patriciarum
3.2.1.73 BglA16
-
 Neocallimastix patriciarum
3.2.1.73 BglA51
-
 Neocallimastix patriciarum
3.2.1.73 BglM2
-
 Neocallimastix patriciarum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 45
-
-
 Neocallimastix patriciarum
3.2.1.73 50
-
-
 Neocallimastix patriciarum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.73 63.06
-
 Barley beta-glucan recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum
3.2.1.73 68.19
-
 Barley beta-glucan recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum
3.2.1.73 83.89
-
 Barley beta-glucan recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum
3.2.1.73 133.3
-
 Barley beta-glucan recombinant enzyme, pH 6.0, 40°C Neocallimastix patriciarum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 6
-
-
 Neocallimastix patriciarum
3.2.1.73 6.5
-
-
 Neocallimastix patriciarum

General Information

EC Number General Information Comment Organism
3.2.1.73 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