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Literature summary for 3.2.1.21 extracted from

  • Sue, M.; Yamazaki, K.; Yajima, S.; Nomura, T.; Matsukawa, T.; Iwamura, H.; Miyamoto, T.
    Molecular and structural characterization of hexameric beta-D-glucosidases in wheat and rye (2006), Plant Physiol., 141, 1237-1247.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.21

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli Secale cereale
isozyme TaGlu1a, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression of wild-type and mutant isozyme TaGlu1a in Escherichia coli Triticum aestivum
isozyme TaGlu1b, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression in Escherichia coli Triticum aestivum
isozyme TaGlu1c, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression in Escherichia coli Triticum aestivum

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant isozyme TaGlu1a, X-ray diffraction structure determination and analysis at 1.8 A resolution Triticum aestivum

Protein Variants

Protein Variants Comment Organism
E191A site-directed mutagenesis, inactive mutant Secale cereale
E191A site-directed mutagenesis, inactive TaGlu1a mutant Triticum aestivum
E407A site-directed mutagenesis, inactive mutant Secale cereale
E407A site-directed mutagenesis, inactive TaGlu1a mutant Triticum aestivum
F198A site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale
F198A site-directed mutagenesis, the mutant shows 24-28fold reduced activity with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one, respectively Secale cereale
F198A site-directed mutagenesis, the TaGlu1a mutant shows reduced activity with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one with highly incresed Km values, respectively Triticum aestivum
F471Y site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale
G464F site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale
G464S site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale
G464S/S465L site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale
S465L site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale
Y378A site-directed mutagenesis, the mutant shows 300-380% increased catalytic eficiency with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one, respectively Secale cereale
Y378F site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme Secale cereale

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 formation of both homo- and heterohexamers by the isozyme Triticum aestivum
additional information
-
 formation of both homo- and heterohexamers by the isozymes Triticum aestivum

Organism

Organism UniProt Comment Textmining
Secale cereale Q9FYS3 isozyme TaGlu1a
-
Triticum aestivum Q1XH04 isozyme TaGlu1c; isozyme TaGlu1c
-
Triticum aestivum Q1XH05 isozyme TaGlu1b; isozyme TaGlu1b
-
Triticum aestivum Q1XIR9 isozyme TaGlu1a; isozyme TaGlu1a
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli by metal affinity chromatography and gel filtration to homogeneity Secale cereale
recombinant wild-type and mutant isozyme TaGlu1a from Escherichia coli by metal affinity chromatography and gel filtration to homogeneity Triticum aestivum

Source Tissue

Source Tissue Comment Organism Textmining
shoot young, isozyme TaGlu1a, isozyme expression profile, overview Triticum aestivum
-
shoot young, isozyme TaGlu1b, isozyme expression profile, overview Triticum aestivum
-
shoot young, isozyme TaGlu1c, isozyme expression profile, overview Triticum aestivum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
245.9
-
 purified native enzyme Triticum aestivum
311.9
-
 purified recombinant His-tagged isozyme TaGlu1a Triticum aestivum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
-
 Secale cereale 2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
 ?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
-
 Triticum aestivum 2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
 ?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O Ser464 and Leu465 are critical in the substrate specificity for the substrate of isozyme TaGlu1a Triticum aestivum 2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
 ?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
-
 Secale cereale 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
 ?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
-
 Triticum aestivum 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
 ?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O Ser464 and Leu465 are critical in the substrate specificity for the substrate of isozyme TaGlu1a Triticum aestivum 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
 ?
4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Triticum aestivum 4-nitrophenol + beta-D-glucose
-
 ?
4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Secale cereale 4-nitrophenol + beta-D-glucose
-
 ?
additional information the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview Triticum aestivum ?
-
 ?
additional information the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview Triticum aestivum ?
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 64085.41, recombinant His-tagged TaGlu1b, SDS-PAGE, gel filtration, and mass spectrometry Triticum aestivum
hexamer 6 * 64141.25, recombinant His-tagged isozyme TaGlu1a, SDS-PAGE, gel filtration, and mass spectrometry Triticum aestivum
hexamer formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview Triticum aestivum
More three-dimensional structure modeling Secale cereale
More formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview Triticum aestivum
More formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview Triticum aestivum

Synonyms

Synonyms Comment Organism
beta-D-glucosidase
-
 Triticum aestivum
beta-D-glucosidase
-
 Secale cereale