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Literature summary for 3.2.1.139 extracted from

  • Siika-aho, M.; Tenkanen, M.; Buchert, J.; Puls, J.; Viikari, L.
    An alpha-glucuronidase from Trichoderma reesei RUT C-30 (1994), Enzyme Microb. Technol., 16, 813-819.
No PubMed abstract available
Search for more literature for 3.2.1.139

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
91000
-
 x * 91000, SDS-PAGE Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei
-
-
-
Trichoderma reesei RUT C-30
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Trichoderma reesei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-O-methyl-glucuronosyl-xylobiose + H2O
-
 Trichoderma reesei 4-O-methyl-glucuronate + xylobiose
-
 ?
4-O-methyl-glucuronosyl-xylobiose + H2O
-
 Trichoderma reesei RUT C-30 4-O-methyl-glucuronate + xylobiose
-
 ?
4-O-methyl-glucuronosyl-xylose + H2O
-
 Trichoderma reesei 4-O-methyl-glucuronate + xylose
-
 ?
4-O-methyl-glucuronosyl-xylose + H2O
-
 Trichoderma reesei RUT C-30 4-O-methyl-glucuronate + xylose
-
 ?
4-O-methyl-glucuronosyl-xylotetraose + H2O
-
 Trichoderma reesei 4-O-methyl-glucuronate + xylotetraose
-
 ?
4-O-methyl-glucuronosyl-xylotetraose + H2O
-
 Trichoderma reesei RUT C-30 4-O-methyl-glucuronate + xylotetraose
-
 ?
4-O-methyl-glucuronosyl-xylotriose + H2O
-
 Trichoderma reesei 4-O-methyl-glucuronate + xylotriose
-
 ?
4-O-methyl-glucuronosyl-xylotriose + H2O
-
 Trichoderma reesei RUT C-30 4-O-methyl-glucuronate + xylotriose
-
 ?
acetylated glucuronoxylan + H2O
-
 Trichoderma reesei ?
-
 ?
additional information enzyme prefers low-molecular-weight xylooligomers as substrates. The enzyme acts almost exclusively on the bond between the terminal xylose at the nonreducing end of the xylose chain and the methyl glucuronic acid attached to it Trichoderma reesei ?
-
 ?
additional information enzyme prefers low-molecular-weight xylooligomers as substrates. The enzyme acts almost exclusively on the bond between the terminal xylose at the nonreducing end of the xylose chain and the methyl glucuronic acid attached to it Trichoderma reesei RUT C-30 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 91000, SDS-PAGE Trichoderma reesei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Trichoderma reesei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 pH 6.2-7.9, stable for 1 h Trichoderma reesei
50
-
 pH 4.8, 24 h, 50% loss of activity Trichoderma reesei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5 6
-
 Trichoderma reesei

pH Range

pH Minimum pH Maximum Comment Organism
3.3 7 pH 3.3: about 60% of maximal activity, pH 7: about 50% of maximal activity Trichoderma reesei

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.8 5.5 40°C, 24 h, stable Trichoderma reesei
6.6
-
 40°C, 24 h, 22% loss of activity Trichoderma reesei