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Literature summary for 3.2.1.73 extracted from

  • Niu, D.; Zhou, X.X.; Yuan, T.Y.; Lin, Z.W.; Ruan, H.; Li, W.F.
    Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum (2010), Biotechnol. Lett., 32, 963-967.
    View publication on PubMed
Search for more literature for 3.2.1.73

Cloned(Commentary)

Cloned (Comment) Organism
gene LicB, expression of mature enzyme and isolated catalytic domain, as well as of the enzyme truncation mutants in Escherichia coli strain BL21 Acetivibrio thermocellus

Protein Variants

Protein Variants Comment Organism
additional information construction of diverse enzyme truncation mutants for domain functional analysis, overview Acetivibrio thermocellus

General Stability

General Stability Organism
Ca2+ stabilizes the enzyme at higher temperatures Acetivibrio thermocellus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Ca2+ stabilizes the enzyme at higher temperatures Acetivibrio thermocellus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Acetivibrio thermocellus lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose ?
-
 ?
additional information Acetivibrio thermocellus ZJL4 lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose ?
-
 ?

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
 gene LicB
-
Acetivibrio thermocellus ZJL4
-
 gene LicB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lichenin + H2O
-
 Acetivibrio thermocellus ?
-
 ?
lichenin + H2O
-
 Acetivibrio thermocellus ZJL4 ?
-
 ?
additional information lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose Acetivibrio thermocellus ?
-
 ?
additional information lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose Acetivibrio thermocellus ZJL4 ?
-
 ?

Subunits

Subunits Comment Organism
More the Thr-Pro box has a positive effect while the dockerin domain has a negative impact on the properties of LicMB. The N-terminal residues 10-25 and C-terminal residues 1-9 of LicMB-CD are necessary to retain high thermostability, while the N-terminal residues 1-7 and C-terminal residues 1-3 are not necessary to maintain enzymatic activity Acetivibrio thermocellus

Synonyms

Synonyms Comment Organism
1,3-1,4-beta-D-glucanase
-
 Acetivibrio thermocellus
Lichenase
-
 Acetivibrio thermocellus
LicMB
-
 Acetivibrio thermocellus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 Ca2+ stabilizes the enzyme at higher temperatures, thermal stability of recombinant wild-type enzyme and mutants in presence and absence of Ca2+, overview Acetivibrio thermocellus
75
-
 purified recombinant wild-type enzyme, 10 min, 51% remaining activity in absence of Ca2+, 86% in presence of 1 mM Ca2+ Acetivibrio thermocellus
80
-
 purified recombinant wild-type enzyme, 5 min, 54% remaining activity in absence of Ca2+, 73% in presence of 1 mM Ca2+ Acetivibrio thermocellus