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Literature summary extracted from

  • Na, H.B.; Jung, W.K.; Jeong, Y.S.; Kim, H.J.; Kim, S.K.; Kim, J.; Yun, H.D.; Lee, J.K.; Kim, H.
    Characterization of a GH family 8 beta-1,3-1,4-glucanase with distinctive broad substrate specificity from Paenibacillus sp. X4 (2015), Biotechnol. Lett., 37, 643-655.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.6 gene bglc8H, DNA and amino acid sequence determination and analysis, phylogenetic tree, cloning in Escherichia coli strain DH5alpha Paenibacillus sp.
3.2.1.73
-
 Paenibacillus sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.6 D156A site-directed mutagenesis, the mutant shows a nearly complete loss of enzyme activity Paenibacillus sp.
3.2.1.6 E95A site-directed mutagenesis, the mutant shows a nearly complete loss of enzyme activity Paenibacillus sp.
3.2.1.73 D156A almost complete loss of activity Paenibacillus sp.
3.2.1.73 Q95A almost complete loss of activity Paenibacillus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.6 Ca2+ activates, 5 mM Ca2+ increases the lichenase activity by 15%. Ca2+ increases the heat stability of the lichenase activity Paenibacillus sp.
3.2.1.73 Ca2+ Ca2+ increases the activity and thermostability of BGlc8H with substrate lichenan Paenibacillus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.6 40000
-
 x * 41561, sequence calculation, x * 40000, SDS-PAGE Paenibacillus sp.
3.2.1.6 41561
-
 x * 41561, sequence calculation, x * 40000, SDS-PAGE Paenibacillus sp.
3.2.1.73 40000
-
-
 Paenibacillus sp.
3.2.1.73 41561
-
-
 Paenibacillus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.6 additional information Paenibacillus sp. the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.6 Paenibacillus sp. A0A088BCU2 clone HB 2-4, gene bglc8H or lic8H
-
3.2.1.73 Paenibacillus sp. A0A088BCU2
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.73 proteolytic modification sequence contains a signal peptide of 31 amino acids Paenibacillus sp.

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.6 native enzyme 10.1fold by anion exchange and hydroxyapatite chromatography Paenibacillus sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.6 2.22
-
 purified native enzyme, pH 5.0, 50°C Paenibacillus sp.
3.2.1.73 2.22
-
 substrate barley beta-D-glucan, pH 5.5, 50°C Paenibacillus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.6 chitosan + H2O
-
 Paenibacillus sp. ?
-
 ?
3.2.1.6 laminarin + H2O
-
 Paenibacillus sp. ?
-
 ?
3.2.1.6 lichenan + H2O
-
 Paenibacillus sp. ?
-
 ?
3.2.1.6 additional information the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan Paenibacillus sp. ?
-
 ?
3.2.1.6 additional information the enzyme hydrolyzes cello-oligosaccharides (G3-G6) to cellotriose and cellobiose but not to D-glucose. Barley beta-glucan and lichenan are hydrolyzed by the enzyme to cellotetraose as the major product Paenibacillus sp. ?
-
 ?
3.2.1.73 barley beta-D-glucan + H2O
-
 Paenibacillus sp. ?
-
 ?
3.2.1.73 carboxymethyl cellulose + H2O 32.2% of the activity with barley beta-D-glucan Paenibacillus sp. ?
-
 ?
3.2.1.73 cellohexaose + H2O
-
 Paenibacillus sp. cellobiose + cellotriose no release of D-glucose ?
3.2.1.73 chitosan + H2O 81.3% of the activity with barley beta-D-glucan Paenibacillus sp. ?
-
 ?
3.2.1.73 laminarin + H2O 4.1% of the activity with barley beta-D-glucan Paenibacillus sp. ?
-
 ?
3.2.1.73 lichenan + H2O 14.5% of the activity with barley beta-D-glucan Paenibacillus sp. ?
-
 ?
3.2.1.73 additional information enzyme hydrolyzes mixed-linked beta-1,3-1,4-glucans and chitosan as well as carboxymethyl cellulose, showing activities of EC 3.2.1.6 and EC 3.2.1.74 Paenibacillus sp. ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.6 ? x * 41561, sequence calculation, x * 40000, SDS-PAGE Paenibacillus sp.
3.2.1.73 ? x * 41561, calculated, x * 40000, SDS-PAGE Paenibacillus sp.

Synonyms

EC Number Synonyms Comment Organism
3.2.1.6 barley-beta-D-glucanase
-
 Paenibacillus sp.
3.2.1.6 beta-1,3-1,4-glucanase
-
 Paenibacillus sp.
3.2.1.6 chitosanase
-
 Paenibacillus sp.
3.2.1.6 CMCase
-
 Paenibacillus sp.
3.2.1.6 laminarinase
-
 Paenibacillus sp.
3.2.1.6 Lic8H
-
 Paenibacillus sp.
3.2.1.6 Lichenase
-
 Paenibacillus sp.
3.2.1.73 Blc8H
-
 Paenibacillus sp.
3.2.1.73 Lic8H
-
 Paenibacillus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.6 50
-
 except for barley-beta-D-glucanase activity with an optimum at 40°C Paenibacillus sp.
3.2.1.73 50
-
-
 Paenibacillus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.6 additional information
-
 Ca2+ increases the heat stability of the lichenase activity retaining 59% activity in the presence of Ca2+ after 15 min of heat treatment at 70°C, compared to 34% in the absence of Ca2+. Ca2+ also increases the heat stability of the beta-glucanase activity (from 18 to 28%). No significant influence of Ca2+ on the heat stability of the chitosanase and CMCase activities are observed Paenibacillus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.6 5
-
 except for chitosanase activity with an optimum at pH 7.0 Paenibacillus sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.6 Paenibacillus sp. sequence calculation
-
 7.61
3.2.1.73 Paenibacillus sp. calculated
-
 7.6

General Information

EC Number General Information Comment Organism
3.2.1.6 evolution the enzyme belongs to glycoside hydrolase family 8 (GH8) and contains A154TDGDMDIAYSLLLADKQW172. The enzyme has a lower ratio of lichenase/barley-beta-D-glucanase activities compared to glycoside hydrolase family GH16 enzymes Paenibacillus sp.
3.2.1.6 additional information Glu95 and Asp156 are catalytically active residues Paenibacillus sp.