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Literature summary for 3.2.1.21 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
Search for more literature for 3.2.1.21

Cloned(Commentary)

Cloned (Comment) Organism
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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

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

Purification (Commentary)

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

Reaction

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Pectobacterium carotovorum

pH Range

pH Minimum pH Maximum Comment Organism
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