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Literature summary extracted from

  • Petersen, B.O.; Krah, M.; Duus, J.O.; Thomsen, K.K.
    A transglycosylating 1,3(4)-beta-glucanase from Rhodothermus marinus. NMR analysis of enzyme reactions (2000), Eur. J. Biochem., 267, 361-369.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.6 lamR gene Rhodothermus marinus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.6 Rhodothermus marinus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.6 recombinant LamR, from transformed Escherichia coli cells Rhodothermus marinus

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 additional information
-
-
Rhodothermus marinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.6 1,3-1,4-beta-D-glucan + H2O LamR cleaves the 1,4-beta-linkages of 3-O-substituted beta-glucose in beta-glucans such as lichenin and 1,3-1,4-beta-glucan from the cell walls of barley endosperm, analysis of reaction products Rhodothermus marinus ?
-
?
3.2.1.6 1,3-beta-oligosaccharide + H2O from DP3 to DP6 Rhodothermus marinus ?
-
?
3.2.1.6 curdlan + H2O from Alcaligenes faecalis, LamR cleaves the 1,3-beta-linkages of 3-O-substituted glucose units in 1,3-beta-glucans such as laminarin and curdlan Rhodothermus marinus ?
-
?
3.2.1.6 laminarin + H2O from Laminaria digitata, LamR cleaves the 1,3-beta-linkages of 3-O-substituted glucose units in 1,3-beta-glucans such as laminarin and curdlan, analysis of reaction products Rhodothermus marinus ?
-
?
3.2.1.6 laminaritriose + H2O
-
Rhodothermus marinus laminaribiose + D-glucose
-
?
3.2.1.6 lichenin + H2O LamR cleaves the 1,4-beta-linkages of 3-O-substituted beta-glucose in beta-glucans such as lichenin, analysis of reaction products Rhodothermus marinus ?
-
?
3.2.1.6 additional information hydrolysis occurs with retention of the beta-configuration at the anomeric carbon, LamR performs transglycosylation to generate both 1,3-beta-glycosidic and 1,4-beta-glycosidic linkages, a laminaribiosyl unit is the minimum requirement for formation of an enzyme-substrate complex and subsequent hydrolysis/transglycosylation, no substrate: laminaribiose Rhodothermus marinus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.6 LamR
-
Rhodothermus marinus
3.2.1.6 More LamR belongs to glycosyl hydrolase family 16 Rhodothermus marinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.6 88
-
-
Rhodothermus marinus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.6 additional information
-
thermostable enzyme Rhodothermus marinus
3.2.1.6 80
-
2 days, stable Rhodothermus marinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.6 5.5
-
-
Rhodothermus marinus