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Literature summary for 3.2.1.78 extracted from

  • Politz, O.; Krah, M.; Thomsen, K.K.; Borriss, R.
    A highly thermostable endo-(1,4)-beta-mannanase from the marine bacterium Rhodothermus marinus (2000), Appl. Microbiol. Biotechnol., 53, 715-721.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Rhodothermus marinus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
113000
-
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da Rhodothermus marinus

Organism

Organism UniProt Comment Textmining
Rhodothermus marinus P49425 ATCC 43812
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carob-galactomannan + H2O i.e. locust bean gum Rhodothermus marinus ?
-
?
guar gum + H2O
-
Rhodothermus marinus ?
-
?
additional information requires at least five sugar moieties for effective catalytic activity, no substrate: yeast mannan Rhodothermus marinus ?
-
?

Subunits

Subunits Comment Organism
? x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da Rhodothermus marinus
More C-terminal domain of 550 amino acid residues with homology to glycosidase family 26 Rhodothermus marinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
-
Rhodothermus marinus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
1 h, 70% residual activity, truncated protein fragments produced in Escherichia coli, 1 h, 87% residual activity, protein derived from Rhodothermus marinus Rhodothermus marinus
90
-
1 h, 25% residual activity, truncated protein fragments produced in Escherichia coli Rhodothermus marinus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
-
Rhodothermus marinus