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Literature summary extracted from

  • Saburi, W.; Kobayashi, M.; Mori, H.; Okuyama, M.; Kimura, A.
    Replacement of the catalytic nucleophile aspartyl residue of dextran glucosidase by cysteine sulfinate enhances transglycosylation activity (2013), J. Biol. Chem., 288, 31670-31677.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.70 dexB, sequence comparisons Streptococcus mutans
3.2.1.70 dexB, sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) CodonPlus RIL Streptococcus mutans

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.70 C129S/C532S site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme, the mutant predominantly catalyzes hydrolysis Streptococcus mutans
3.2.1.70 D194A/C129S/C532S site-directed mutagenesis Streptococcus mutans
3.2.1.70 D194C/C129S/C532S site-directed mutagenesis, the mutant shows highly reduced activity compared with the wild-type enzyme and mutant C129S/C532S, oxidation with KI activates the mutant by 330fold which is 0.27% activity of the activity of mutant C129S/C532S, the oxidized mutant Ox-D194C-2CS catalyzes both hydrolysis and transglucosylation Streptococcus mutans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.70 additional information
-
 additional information detailed steady-state kinetics of wild-type and mutant enzymes, overview Streptococcus mutans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.70 additional information Streptococcus mutans dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran ?
-
 ?
3.2.1.70 additional information Streptococcus mutans ATCC 700610 dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.70 Streptococcus mutans Q2HWU5 gene dexB; gene dexB
-
3.2.1.70 Streptococcus mutans Q99040 gene dexB; gene dexB
-
3.2.1.70 Streptococcus mutans Q99040 gene dexB; serotype C, gene dexB
-
3.2.1.70 Streptococcus mutans ATCC 700610 Q99040 gene dexB; serotype C, gene dexB
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.70 4-nitrophenyl-alpha-D-glucopyranoside + H2O
-
 Streptococcus mutans 4-nitrophenol + D-glucose
-
 ?
3.2.1.70 4-nitrophenyl-alpha-D-glucopyranoside + H2O
-
 Streptococcus mutans ATCC 700610 4-nitrophenol + D-glucose
-
 ?
3.2.1.70 4-nitrophenyl-alpha-isomaltoside + H2O
-
 Streptococcus mutans 4-nitrophenol + isomaltose
-
 ?
3.2.1.70 4-nitrophenyl-alpha-isomaltoside + H2O
-
 Streptococcus mutans ATCC 700610 4-nitrophenol + isomaltose
-
 ?
3.2.1.70 additional information dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran Streptococcus mutans ?
-
 ?
3.2.1.70 additional information the enzyme also performs transglucosylation Streptococcus mutans ?
-
 ?
3.2.1.70 additional information dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran Streptococcus mutans ATCC 700610 ?
-
 ?
3.2.1.70 additional information the enzyme also performs transglucosylation Streptococcus mutans ATCC 700610 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.70 dextran glucosidase
-
 Streptococcus mutans
3.2.1.70 SMDG
-
 Streptococcus mutans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.70 37
-
 assay at Streptococcus mutans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.70 6
-
 assay at Streptococcus mutans

General Information

EC Number General Information Comment Organism
3.2.1.70 evolution the enzyme belongs to the glycosyl hydrolase family 13 Streptococcus mutans
3.2.1.70 evolution the enzyme belongs to the glycosyl hydrolase family 13, GH13 Streptococcus mutans
3.2.1.70 additional information the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532 Streptococcus mutans
3.2.1.70 additional information the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532. Asp194 is essential for enzyme activity Streptococcus mutans