Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kim, D.; Han, M.; Oh, H.; Park, D.; Kim, S.; Lee, S.; Shin, D.; Son, K.; Bae, K.; Park, H.
    Catalytic properties of a GH10 endo-beta-1,4-xylanase from Streptomyces thermocarboxydus HY-15 isolated from the gut of Eisenia fetida (2010), J. Mol. Catal. B, 62, 32-39.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.8 DTT 23% activation at 5 mM Streptomyces thermocarboxydus
3.2.1.8 Triton X-100 42% activation at 0.5% Streptomyces thermocarboxydus
3.2.1.8 Tween-80 38% activation at 0.5% Streptomyces thermocarboxydus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 gene xylG, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21 Streptomyces thermocarboxydus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 Ca2+ 7% inhibition at 1 mM Streptomyces thermocarboxydus
3.2.1.8 Cu2+ 77% inhibition at 1 mM Streptomyces thermocarboxydus
3.2.1.8 EDTA 59% inhibition at 5 mM Streptomyces thermocarboxydus
3.2.1.8 Hg2+ complete inhibition at 1 mM Streptomyces thermocarboxydus
3.2.1.8 iodoacetamide 59% inhibition at 5 mM Streptomyces thermocarboxydus
3.2.1.8 N-bromosuccimide complete inhibition at 5 mM Streptomyces thermocarboxydus
3.2.1.8 NEM 49% inhibition at 5 mM Streptomyces thermocarboxydus
3.2.1.8 Sodium azide 43% inhibition at 5 mM Streptomyces thermocarboxydus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.8 additional information
-
 additional information Michaelis-Menten kinetics Streptomyces thermocarboxydus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.8 Co2+ 27% activation at 1 mM Streptomyces thermocarboxydus
3.2.1.8 Fe2+ 16% activation at 1 mM Streptomyces thermocarboxydus
3.2.1.8 Mn2+ 42% activation at 1 mM Streptomyces thermocarboxydus
3.2.1.8 additional information no effect by Ca2+, Sn2+, Ba2+, Ni2+, Zn2+, and Mg2+ at 1 mM, and by 2-mercaptoethanol at 5 mM Streptomyces thermocarboxydus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 43962
-
 x * 43962, sequence calculation Streptomyces thermocarboxydus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O Streptomyces thermocarboxydus
-
 ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O Streptomyces thermocarboxydus HY-15
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Streptomyces thermocarboxydus C6ZHB0 isolated from the gut of Eisenia fetida, gene xylG
-
3.2.1.8 Streptomyces thermocarboxydus HY-15 C6ZHB0 isolated from the gut of Eisenia fetida, gene xylG
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 recombinant His-tagged enzyme from Escherichia coli strain BVL21 by affinity chromatography Streptomyces thermocarboxydus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 additional information
-
 substrate specificity, overview Streptomyces thermocarboxydus
3.2.1.8 70.3
-
 purified enzyme, substrate is xylan from birchwood Streptomyces thermocarboxydus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 4-nitrophenyl cellobioside + H2O high activity Streptomyces thermocarboxydus 4-nitrophenol + cellobiose
-
 ?
3.2.1.8 4-nitrophenyl cellobioside + H2O high activity Streptomyces thermocarboxydus HY-15 4-nitrophenol + cellobiose
-
 ?
3.2.1.8 beta-1,4-xylan + H2O
-
 Streptomyces thermocarboxydus ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O from oat spelt, birchwood, or beechwood in descending order Streptomyces thermocarboxydus ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O
-
 Streptomyces thermocarboxydus HY-15 ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O from oat spelt, birchwood, or beechwood in descending order Streptomyces thermocarboxydus HY-15 ?
-
 ?
3.2.1.8 additional information substrate specificity, overview Streptomyces thermocarboxydus ?
-
 ?
3.2.1.8 additional information substrate specificity, overview Streptomyces thermocarboxydus HY-15 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 ? x * 43962, sequence calculation Streptomyces thermocarboxydus
3.2.1.8 More structure homology modelling, XylG folds to form an (alpha/beta)8-barrel with two catalytic residues of an acid/base Glu181 and a nucleophile Glu289. The formation of a disulfide bond between Cys321 and Cys327 is predicted by homology modeling Streptomyces thermocarboxydus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 GH10 endo-beta-1,4-xylanase
-
 Streptomyces thermocarboxydus
3.2.1.8 More the enzyme belongs to the glycosyl hydrolase family 10, GH10 Streptomyces thermocarboxydus
3.2.1.8 XylG
-
 Streptomyces thermocarboxydus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 55
-
 recombinant enzyme Streptomyces thermocarboxydus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.8 35 75 activity range Streptomyces thermocarboxydus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 6
-
 recombinant enzyme Streptomyces thermocarboxydus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 4.5 10.5 activity range, over 85% of its maximum activity at a pH range of pH 5.0 to pH 6.5 Streptomyces thermocarboxydus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.8 Streptomyces thermocarboxydus sequence calculation
-
 6.74