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

BRENDA support

Literature summary extracted from

  • Berezina, O.V.; Herlet, J.; Rykov, S.V.; Kornberger, P.; Zavyalov, A.; Kozlov, D.; Sakhibgaraeva, L.; Krestyanova, I.; Schwarz, W.H.; Zverlov, V.V.; Liebl, W.; Yarotsky, S.V.
    Thermostable multifunctional GH74 xyloglucanase from Myceliophthora thermophila high-level expression in Pichia pastoris and characterization of the recombinant protein (2017), Appl. Microbiol. Biotechnol., 101, 5653-5666 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.151 codon-optimized gene MYCTH_116384, the sequence of mtXgh74 is shown to be identical to MYCTH_116384, formation of synthetic mt74syn gene, recombinant expression of highly glycosylated extracellular enzyme in Pichia pastoris strains GS115 and VKPM Y-4269, respectively, the enzyme is secreted Thermothelomyces thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.151 Al3+ 70% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 Cd2+ 20% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 Co2+ 10% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 Cu2+ 30% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 Fe2+ 30% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 additional information no or poor effects by 5 mM of EDTA Thermothelomyces thermophilus
3.2.1.151 NH4Cl 10% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 Pb2+ 70% inhibition at 5 mM Thermothelomyces thermophilus
3.2.1.151 Zn2+ 10% inhibition at 5 mM Thermothelomyces thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.151 extracellular
-
 Thermothelomyces thermophilus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.151 additional information no or poor effetcs by 5 mM of Ca2+, Mn2+, Mg2+, and Ba2+ Thermothelomyces thermophilus
3.2.1.151 Ni2+ slight activation at 5 mM Thermothelomyces thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.151 Thermothelomyces thermophilus G2QHR7
-
-
3.2.1.151 Thermothelomyces thermophilus ATCC 42464 G2QHR7
-
-
3.2.1.151 Thermothelomyces thermophilus VKPM F-244 G2QHR7
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.151 glycoprotein the secreted enzyme contains one potential N-glycosylation site, deglycosylation with N-glycosidase Endo H Thermothelomyces thermophilus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.151 partially recombinant extracellular enzyme from Pichia pastoris strains GS115 and recombinant enzyme expressed from mt74syn gene in Pichia pastoris strain VKPM Y-4269 by ethanol precipitation and dialysis Thermothelomyces thermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.151 55
-
 crude extracellular recombinant enzyme, pH 6.0, 60°C with 0.5% soluble or 1% insoluble polysaccharide substrate Thermothelomyces thermophilus
3.2.1.151 80
-
 partially purified recombinant enzyme, pH 6.0, 60°C with 0.5% soluble or 1% insoluble polysaccharide substrate Thermothelomyces thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.151 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-D-Glc + H2O
-
 Thermothelomyces thermophilus ?
-
 ?
3.2.1.151 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-D-Glc + H2O
-
 Thermothelomyces thermophilus ?
-
 ?
3.2.1.151 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-D-Glc + H2O
-
 Thermothelomyces thermophilus ?
-
 ?
3.2.1.151 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-D-Glc + H2O
-
 Thermothelomyces thermophilus ATCC 42464 ?
-
 ?
3.2.1.151 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-D-Glc + H2O
-
 Thermothelomyces thermophilus VKPM F-244 ?
-
 ?
3.2.1.151 barley beta-glucan + H2O 4% activity compared to tamarind seed xyloglucan Thermothelomyces thermophilus ?
-
 ?
3.2.1.151 barley beta-glucan + H2O 4% activity compared to tamarind seed xyloglucan Thermothelomyces thermophilus ATCC 42464 ?
-
 ?
3.2.1.151 barley beta-glucan + H2O 4% activity compared to tamarind seed xyloglucan Thermothelomyces thermophilus VKPM F-244 ?
-
 ?
3.2.1.151 carboxymethylcellulose + H2O 2% activity compared to tamarind seed xyloglucan Thermothelomyces thermophilus ?
-
 ?
3.2.1.151 carboxymethylcellulose + H2O 2% activity compared to tamarind seed xyloglucan Thermothelomyces thermophilus ATCC 42464 ?
-
 ?
3.2.1.151 carboxymethylcellulose + H2O 2% activity compared to tamarind seed xyloglucan Thermothelomyces thermophilus VKPM F-244 ?
-
 ?
3.2.1.151 additional information enzyme MtXgh74 shows an endoprocessive mode of action. Oligosaccharides XXXG, XXLG, and XLXG are completely hydrolyzed at the end of the reaction, whereas XLLG oligosaccharide is not hydrolyzed Thermothelomyces thermophilus ?
-
 ?
3.2.1.151 additional information enzyme MtXgh74 shows an endoprocessive mode of action. Oligosaccharides XXXG, XXLG, and XLXG are completely hydrolyzed at the end of the reaction, whereas XLLG oligosaccharide is not hydrolyzed Thermothelomyces thermophilus ATCC 42464 ?
-
 ?
3.2.1.151 additional information enzyme MtXgh74 shows an endoprocessive mode of action. Oligosaccharides XXXG, XXLG, and XLXG are completely hydrolyzed at the end of the reaction, whereas XLLG oligosaccharide is not hydrolyzed Thermothelomyces thermophilus VKPM F-244 ?
-
 ?
3.2.1.151 tamarind seed xyloglucan + H2O best substrate, enzyme MtXgh74 hydrolyzes various linkages within the xyloglucan building blocks XXXG, XXLG, and XLXG (except XLLG) producing diverse low molecular weight oligosaccharides Thermothelomyces thermophilus xylooligosaccharides
-
 ?
3.2.1.151 tamarind seed xyloglucan + H2O best substrate, enzyme MtXgh74 hydrolyzes various linkages within the xyloglucan building blocks XXXG, XXLG, and XLXG (except XLLG) producing diverse low molecular weight oligosaccharides Thermothelomyces thermophilus ATCC 42464 xylooligosaccharides
-
 ?
3.2.1.151 tamarind seed xyloglucan + H2O best substrate, enzyme MtXgh74 hydrolyzes various linkages within the xyloglucan building blocks XXXG, XXLG, and XLXG (except XLLG) producing diverse low molecular weight oligosaccharides Thermothelomyces thermophilus VKPM F-244 xylooligosaccharides
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.151 ? x * 80000, recombinant glycosylated enzyme, SDS-PAGE, x * 77000, recombinant deglycosylated enzyme, SDS-PAGE Thermothelomyces thermophilus
3.2.1.151 More MALDI-TOF mass spectrometry peptide fingerprinting, enzyme sequences comparisons Thermothelomyces thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.151 endo-processive xyloglucanase
-
 Thermothelomyces thermophilus
3.2.1.151 GH74 xyloglucanase
-
 Thermothelomyces thermophilus
3.2.1.151 MtXgh74
-
 Thermothelomyces thermophilus
3.2.1.151 MYCTH_116384
-
 Thermothelomyces thermophilus
3.2.1.151 Xgl74A
-
 Thermothelomyces thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.151 70 75 recombinant enzyme Thermothelomyces thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.151 40 85 recombinant enzyme, activity range, prodile overview Thermothelomyces thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.151 50
-
 recombinant enzyme, pH 6.0, 3 h, the enzyme retains 100% of its activity Thermothelomyces thermophilus
3.2.1.151 60
-
 recombinant enzyme, pH 6.0, half-life is 40 min Thermothelomyces thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.151 6.5
-
 recombinant enzyme Thermothelomyces thermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.151 3.5 10 recombinant enzyme, activity range, prodile overview Thermothelomyces thermophilus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.151 5 8.5 recombinant enzyme, over 50% activity remaining within this range Thermothelomyces thermophilus

General Information

EC Number General Information Comment Organism
3.2.1.151 evolution the enzyme belongs to the glycosyl hydrolase family 74, GH74. Myceliophthora thermophila strain VKPM F-244 produces two xyloglucan-degrading proteins with MWs of about 24 and 80 kDa. The 80 kDa protein is subjected to MALDI-TOF mass spectrometry peptide fingerprinting. Analysis of the data reveals maximal homology with the putative GH74 xyloglucanase from Myceliophthora thermophila ATCC 42464. The mtXgh74 gene encoding a GH74 xyloglucanase from strain VKPM F-244 is isolated using primers designed on the base of the MYCTH_116384 gene encoding AEO58927.1. The sequence of mtXgh74 is shown to be identical to MYCTH_116384 Thermothelomyces thermophilus
3.2.1.151 physiological function a molecule of tamarind xyloglucan has a certain structural regularity: it is composed of 1,4-beta-D-glucotetraose units, where three glucosyl residues modified with a D-xylose via alpha-1,6-glycosidic bonds are followed by an unbranched glucosyl residue. The D-xyloses may be decorated with beta-1,2-D-galactosyl or to small amounts with alpha-1,2-L-arabinosyl residues. Degradation of xyloglucan requires a broad range of hydrolases with different activities and specificities, including extracellular Xgh74 endoxyloglucanase Thermothelomyces thermophilus