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Literature summary extracted from

  • Matsuzawa, T.; Watanabe, M.; Kameda, T.; Kameyama, A.; Yaoi, K.
    Cooperation between beta-galactosidase and an isoprimeverose-producing oligoxyloglucan hydrolase is key for xyloglucan degradation in Aspergillus oryzae (2019), FEBS J., 286, 3182-3193 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.23 expression in Pichia pastoris Aspergillus oryzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.23 1.42
-
4-nitrophenyl beta-D-galactopyranoside pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 1.76
-
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 2.41
-
beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 104
-
lactose pH 4.5, 60°C Aspergillus oryzae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.23 122000
-
SDS-PAGE, recombinant glycosylated enzyme Aspergillus oryzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.23 xyloglucan oligosaccharide + H2O Aspergillus oryzae the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex galactopyranose + xyloglucan oligosaccharide
-
?
3.2.1.23 xyloglucan oligosaccharide + H2O Aspergillus oryzae ATCC 42149 the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex galactopyranose + xyloglucan oligosaccharide
-
?
3.2.1.120 xyloglucan + H2O Aspergillus oryzae the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex isoprimeverose + ?
-
?
3.2.1.120 xyloglucan + H2O Aspergillus oryzae ATCC 42149 the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex isoprimeverose + ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.23 Aspergillus oryzae Q2UCU3
-
-
3.2.1.23 Aspergillus oryzae ATCC 42149 Q2UCU3
-
-
3.2.1.120 Aspergillus oryzae Q2U8V9
-
-
3.2.1.120 Aspergillus oryzae ATCC 42149 Q2U8V9
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.23 glycoprotein recombinant LacA is N-glycosylated and the protein band is shifted from approximately 122000 Da to 108000 Da by endoglycosidase Hf treatment Aspergillus oryzae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.23 recombinant His6-tagged enzyme Aspergillus oryzae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.23 3 3.9 substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 17.7
-
substrate: lactose, pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 35.8
-
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 71
-
substrate: beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 121
-
substrate: beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 299
-
substrate: 4-nitrophenyl beta-D-galactopyranoside, pH 4.5, 60°C Aspergillus oryzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.23 4-nitrophenyl beta-D-galactopyranoside + H2O
-
Aspergillus oryzae 4-nitrophenol + beta-D-galactopyranose
-
?
3.2.1.23 4-nitrophenyl beta-D-galactopyranoside + H2O
-
Aspergillus oryzae ATCC 42149 4-nitrophenol + beta-D-galactopyranose
-
?
3.2.1.23 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
-
Aspergillus oryzae alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + beta-D-galactose
-
?
3.2.1.23 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
-
Aspergillus oryzae ATCC 42149 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + beta-D-galactose
-
?
3.2.1.23 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
-
Aspergillus oryzae alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + beta-D-galactose
-
?
3.2.1.23 beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc + H2O
-
Aspergillus oryzae alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc + beta-D-galactose
-
?
3.2.1.23 beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
-
Aspergillus oryzae alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + beta-D-galactose
-
?
3.2.1.23 lactose + H2O
-
Aspergillus oryzae D-glucose + D-galactose
-
?
3.2.1.23 lactose + H2O
-
Aspergillus oryzae ATCC 42149 D-glucose + D-galactose
-
?
3.2.1.23 xyloglucan oligosaccharide + H2O the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex Aspergillus oryzae galactopyranose + xyloglucan oligosaccharide
-
?
3.2.1.23 xyloglucan oligosaccharide + H2O the enzyme cleaves galactopyranosyl residues from xyloglucan oligosaccharides, but not from xyloglucan polysaccharide. An isoprimeverose unit at the nonreducing end of the main chain of xyloglucan oligosaccharides blocks LacA activity Aspergillus oryzae galactopyranose + xyloglucan oligosaccharide
-
?
3.2.1.23 xyloglucan oligosaccharide + H2O the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex Aspergillus oryzae ATCC 42149 galactopyranose + xyloglucan oligosaccharide
-
?
3.2.1.23 xyloglucan oligosaccharide + H2O the enzyme cleaves galactopyranosyl residues from xyloglucan oligosaccharides, but not from xyloglucan polysaccharide. An isoprimeverose unit at the nonreducing end of the main chain of xyloglucan oligosaccharides blocks LacA activity Aspergillus oryzae ATCC 42149 galactopyranose + xyloglucan oligosaccharide
-
?
3.2.1.120 xyloglucan + H2O the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex Aspergillus oryzae isoprimeverose + ?
-
?
3.2.1.120 xyloglucan + H2O isoprimeverose-producing oligoxyloglucan hydrolase requires LacA for the removal of galactopyranosyl residues Aspergillus oryzae isoprimeverose + ?
-
?
3.2.1.120 xyloglucan + H2O the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex Aspergillus oryzae ATCC 42149 isoprimeverose + ?
-
?
3.2.1.120 xyloglucan + H2O isoprimeverose-producing oligoxyloglucan hydrolase requires LacA for the removal of galactopyranosyl residues Aspergillus oryzae ATCC 42149 isoprimeverose + ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.23 LacA
-
Aspergillus oryzae
3.2.1.120 IpeA
-
Aspergillus oryzae
3.2.1.120 isoprimeverose-producing oligoxyloglucan hydrolase
-
Aspergillus oryzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.23 60
-
-
Aspergillus oryzae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.23 65
-
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 289
-
beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 525
-
4-nitrophenyl beta-D-galactopyranoside pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 869
-
lactose pH 4.5, 60°C Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.23 4.5
-
-
Aspergillus oryzae

Expression

EC Number Organism Comment Expression
3.2.1.23 Aspergillus oryzae expression of the lacA gene is repressed by D-glucose down
3.2.1.23 Aspergillus oryzae induced in the presence of xyloglucan oligosaccharides up

General Information

EC Number General Information Comment Organism
3.2.1.23 physiological function the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA -xyloglucan oligosaccharide complex Aspergillus oryzae
3.2.1.120 physiological function the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex Aspergillus oryzae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.23 8.36
-
lactose pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 37
-
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 120
-
beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc pH 4.5, 60°C Aspergillus oryzae
3.2.1.23 370
-
4-nitrophenyl beta-D-galactopyranoside pH 4.5, 60°C Aspergillus oryzae