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Literature summary for 3.2.1.151 extracted from
- 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 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Al3+ | 70% inhibition at 5 mM | Thermothelomyces thermophilus |  |
| Cd2+ | 20% inhibition at 5 mM | Thermothelomyces thermophilus | |
| Co2+ | 10% inhibition at 5 mM | Thermothelomyces thermophilus | |
| Cu2+ | 30% inhibition at 5 mM | Thermothelomyces thermophilus | |
| Fe2+ | 30% inhibition at 5 mM | Thermothelomyces thermophilus | |
| additional information | no or poor effects by 5 mM of EDTA | Thermothelomyces thermophilus | |
| NH4Cl | 10% inhibition at 5 mM | Thermothelomyces thermophilus | |
| Pb2+ | 70% inhibition at 5 mM | Thermothelomyces thermophilus | |
| Zn2+ | 10% inhibition at 5 mM | Thermothelomyces thermophilus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Thermothelomyces thermophilus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no or poor effetcs by 5 mM of Ca2+, Mn2+, Mg2+, and Ba2+ | Thermothelomyces thermophilus | |
| Ni2+ | slight activation at 5 mM | Thermothelomyces thermophilus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermothelomyces thermophilus | G2QHR7 | - |
- |
| Thermothelomyces thermophilus ATCC 42464 | G2QHR7 | - |
- |
| Thermothelomyces thermophilus VKPM F-244 | G2QHR7 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the secreted enzyme contains one potential N-glycosylation site, deglycosylation with N-glycosidase Endo H | Thermothelomyces thermophilus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 55 | - |
crude extracellular recombinant enzyme, pH 6.0, 60°C with 0.5% soluble or 1% insoluble polysaccharide substrate | Thermothelomyces thermophilus |
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| barley beta-glucan + H2O | 4% activity compared to tamarind seed xyloglucan | Thermothelomyces thermophilus | ? | - |
? | |
| barley beta-glucan + H2O | 4% activity compared to tamarind seed xyloglucan | Thermothelomyces thermophilus ATCC 42464 | ? | - |
? | |
| barley beta-glucan + H2O | 4% activity compared to tamarind seed xyloglucan | Thermothelomyces thermophilus VKPM F-244 | ? | - |
? | |
| carboxymethylcellulose + H2O | 2% activity compared to tamarind seed xyloglucan | Thermothelomyces thermophilus | ? | - |
? | |
| carboxymethylcellulose + H2O | 2% activity compared to tamarind seed xyloglucan | Thermothelomyces thermophilus ATCC 42464 | ? | - |
? | |
| carboxymethylcellulose + H2O | 2% activity compared to tamarind seed xyloglucan | Thermothelomyces thermophilus VKPM F-244 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 80000, recombinant glycosylated enzyme, SDS-PAGE, x * 77000, recombinant deglycosylated enzyme, SDS-PAGE | Thermothelomyces thermophilus |
| More | MALDI-TOF mass spectrometry peptide fingerprinting, enzyme sequences comparisons | Thermothelomyces thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-processive xyloglucanase | - |
Thermothelomyces thermophilus |
| GH74 xyloglucanase | - |
Thermothelomyces thermophilus |
| MtXgh74 | - |
Thermothelomyces thermophilus |
| MYCTH_116384 | - |
Thermothelomyces thermophilus |
| Xgl74A | - |
Thermothelomyces thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | 75 | recombinant enzyme | Thermothelomyces thermophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 85 | recombinant enzyme, activity range, prodile overview | Thermothelomyces thermophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
recombinant enzyme, pH 6.0, 3 h, the enzyme retains 100% of its activity | Thermothelomyces thermophilus |
| 60 | - |
recombinant enzyme, pH 6.0, half-life is 40 min | Thermothelomyces thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
recombinant enzyme | Thermothelomyces thermophilus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 10 | recombinant enzyme, activity range, prodile overview | Thermothelomyces thermophilus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8.5 | recombinant enzyme, over 50% activity remaining within this range | Thermothelomyces thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
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Release 2023.1 (January 2023)
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