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Literature summary extracted from

  • Mao, S.; Lu, Z.; Zhang, C.; Lu, F.; Bie, X.
    Purification, characterization, and heterologous expression of a thermostable beta-1,3-1,4-glucanase from Bacillus altitudinis YC-9 (2013), Appl. Biochem. Biotechnol., 169, 960-975.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis. Recombinant expression of the enzyme fused to the Trx-tag/His-tag/S-tag sequences in Escherichia coli strain BL21 (DE3), the enzyme is located in the cell lysate and the cell culture supernatant Bacillus altitudinis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.73 Cu2+
-
Bacillus altitudinis
3.2.1.73 EDTA
-
Bacillus altitudinis
3.2.1.73 Mn2+
-
Bacillus altitudinis
3.2.1.73 Zn2+ slightly inhibitory Bacillus altitudinis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.73 Ca2+ activates slightly Bacillus altitudinis
3.2.1.73 Co2+ activates Bacillus altitudinis
3.2.1.73 Fe2+ activates Bacillus altitudinis
3.2.1.73 additional information no or poor effects by K+, Na+, and Mg2+ Bacillus altitudinis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.73 27470
-
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE Bacillus altitudinis
3.2.1.73 45000
-
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE Bacillus altitudinis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.73 lichenan + H2O Bacillus altitudinis
-
?
-
?
3.2.1.73 lichenan + H2O Bacillus altitudinis YC-9
-
?
-
?
3.2.1.73 additional information Bacillus altitudinis beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans ?
-
?
3.2.1.73 additional information Bacillus altitudinis YC-9 beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Bacillus altitudinis K7XFI7 isolated from spring silt
-
3.2.1.73 Bacillus altitudinis YC-9 K7XFI7 isolated from spring silt
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.73 native enzyme 37fold from strain YC-9 by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration, recombinant enzyme from Escherichia coli strain BL21 (DE3) cell culture supernatant by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration Bacillus altitudinis

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 2373
-
purified native enzyme, pH 6.0, 65°C Bacillus altitudinis
3.2.1.73 5393
-
purified recombinant enzyme, pH 6.0, 65°C Bacillus altitudinis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 lichenan + H2O
-
Bacillus altitudinis ?
-
?
3.2.1.73 lichenan + H2O
-
Bacillus altitudinis YC-9 ?
-
?
3.2.1.73 additional information beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans Bacillus altitudinis ?
-
?
3.2.1.73 additional information native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan Bacillus altitudinis ?
-
?
3.2.1.73 additional information beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans Bacillus altitudinis YC-9 ?
-
?
3.2.1.73 additional information native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan Bacillus altitudinis YC-9 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.73 ? x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE Bacillus altitudinis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 beta-1,3-1,4-glucanase
-
Bacillus altitudinis
3.2.1.73 Lichenase
-
Bacillus altitudinis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 65
-
native and recombinant enzyme Bacillus altitudinis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.73 40 80 activity profile, overview Bacillus altitudinis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.73 60
-
purified recombinant enzyme, retains more than 90% activity after 2 h Bacillus altitudinis
3.2.1.73 70
-
purified recombinant enzyme, retains more 75% activity after 10 min Bacillus altitudinis
3.2.1.73 80
-
purified recombinant enzyme, retains more 44% activity after 10 min Bacillus altitudinis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 6
-
recombinant enzyme Bacillus altitudinis