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Literature summary extracted from

  • An, C.L.; Lim, W.J.; Hong, S.Y.; Kim, E.J.; Shin, E.C.; Kim, M.K.; Lee, J.R.; Park, S.R.; Woo, J.G.; Lim, Y.P.; Yun, H.D.
    Analysis of bgl operon structure and characterization of beta-glucosidase from Pectobacterium carotovorum subsp. carotovorum LY34 (2004), Biosci. Biotechnol. Biochem., 68, 2270-2278.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.21 bgl operon, gene bglB, contruction of a genomic library, DNA and amino acid sequence determination and analysis, determination of bgl operon structure and organization, overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) as His-tagged proteins, subcloning in Escherichia coli strain DH5alpha Pectobacterium carotovorum

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.21 E173A site-directed mutagenesis, inactive mutant Pectobacterium carotovorum
3.2.1.21 E362A site-directed mutagenesis, inactive mutant Pectobacterium carotovorum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.21 Co2+ 85% inhibition at 2 mM Pectobacterium carotovorum
3.2.1.21 Cu2+ 95% inhibition at 2 mM Pectobacterium carotovorum
3.2.1.21 Hg2+ complete inhibition at 2 mM Pectobacterium carotovorum
3.2.1.21 Mn2+ 28% inhibition at 2 mM Pectobacterium carotovorum
3.2.1.21 Zn2+ 95% inhibition at 2 mM Pectobacterium carotovorum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.21 0.25
-
4-nitrophenyl beta-D-glucopyranoside pH 7.0, 40°C, recombinant enzyme Pectobacterium carotovorum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.21 Mg2+ activates, maximal at 15 mM, 20% activation at 2 mM Pectobacterium carotovorum
3.2.1.21 additional information no effect by Ca2+ at 2 mM Pectobacterium carotovorum

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Pectobacterium carotovorum Q6QGY5 ssp. carotovorum, strain LY34, bgl operon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.21 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Pectobacterium carotovorum

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.21 celloheptaose + 6 H2O = 7 beta-D-glucose residues E173 and E362 are essential for catalytic activity Pectobacterium carotovorum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.21 553
-
purified recombinant enzyme, substrate 4-nitrophenyl beta-D-glucopyranoside Pectobacterium carotovorum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O hydrolysis of beta-linkages Pectobacterium carotovorum 4-nitrophenol + beta-D-glucose
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.21 40
-
-
Pectobacterium carotovorum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.21 20 50 25% of maximal activity at 20°C and 50°C, half-maximal activity at 28°C and 46°C Pectobacterium carotovorum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.21 40
-
loss of 40% of activity within 50 min Pectobacterium carotovorum
3.2.1.21 50
-
loss of 90% of activity within 20 min Pectobacterium carotovorum
3.2.1.21 60
-
inactivation within 20 min Pectobacterium carotovorum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 7
-
-
Pectobacterium carotovorum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.21 4 9 20% of maximal activity at pH 5.0 and pH 9.0, half-maximal activity at pH 5.5 and pH 8.5 Pectobacterium carotovorum