EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.4 | Co2+ | 20.6% activation at 1 mM | Pseudoalteromonas sp. DY3 | |
3.2.1.4 | Mn2+ | 28.8% activation at 1 mM | Pseudoalteromonas sp. DY3 | |
3.2.1.8 | additional information | the enzyme activity is not affected by EDTA | Thermothelomyces thermophilus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.4 | gene celX, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Pseudoalteromonas sp. DY3 |
3.2.1.8 | gene MYCTH_49824, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain X33 under control of an AOX1 promoter | Thermothelomyces thermophilus |
3.2.1.8 | gene MYCTH_56237, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain X33 under control of an AOX1 promoter | Thermothelomyces thermophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.4 | Cu2+ | 6.5% inhibition at 1 mM | Pseudoalteromonas sp. DY3 | |
3.2.1.4 | Pb2+ | 14.9% inhibition at 1 mM | Pseudoalteromonas sp. DY3 | |
3.2.1.8 | Cu2+ | - |
Thermothelomyces thermophilus | |
3.2.1.8 | additional information | the enzyme activity is not affected by EDTA; the enzyme activity is not affected by EDTA | Thermothelomyces thermophilus | |
3.2.1.8 | Ni2+ | - |
Thermothelomyces thermophilus | |
3.2.1.8 | Zn2+ | - |
Thermothelomyces thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.4 | additional information | - |
additional information | Km for carboxymethyl cellulose is 6.4 mg/ml, pH 5.5, 45°C, recombinant enzyme, Michaelis-Menten kinetics | Pseudoalteromonas sp. DY3 | |
3.2.1.8 | additional information | - |
additional information | Km is 5.67 mg/ml | Thermothelomyces thermophilus | |
3.2.1.8 | additional information | - |
additional information | Km is 8.80 mg/ml | Thermothelomyces thermophilus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.4 | additional information | no or poor effect by 1 mM of Mg2+, Ba2+, Zn2+, Ca2+, and Ni2+ | Pseudoalteromonas sp. DY3 | |
3.2.1.8 | Mg2+ | activates | Thermothelomyces thermophilus | |
3.2.1.8 | Mn2+ | activates | Thermothelomyces thermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.4 | Pseudoalteromonas sp. DY3 | - |
- |
- |
3.2.1.8 | Thermothelomyces thermophilus | G2QDB9 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus | G2QIK8 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus ATCC 42464 | G2QDB9 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus ATCC 42464 | G2QIK8 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus BCRC 31852 | G2QDB9 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus BCRC 31852 | G2QIK8 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus DSM 1799 | G2QDB9 | i.e. Sporotrichum thermophile | - |
3.2.1.8 | Thermothelomyces thermophilus DSM 1799 | G2QIK8 | i.e. Sporotrichum thermophile | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.2.1.8 | glycoprotein | MYCTH_49824 has one O-glycosylation site (at residue 40) and four N-glycosylation sites (resides 20, 33, 101, 107) | Thermothelomyces thermophilus |
3.2.1.8 | glycoprotein | MYCTH_56237 has two putative O-glycosylation sites (residues 35 and 37) and one N-glycosylation site (Asn22) | Thermothelomyces thermophilus |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.4 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Pseudoalteromonas sp. DY3 |
3.2.1.8 | recombinant His-tagged enzyme from Pichia pastoris strain X33 by nickel affinity chromatography | Thermothelomyces thermophilus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 1412.5 | - |
purified recombinant enzyme, pH 7.0, 60°C | Thermothelomyces thermophilus |
3.2.1.8 | 1533.7 | - |
purified recombinant enzyme, pH 6.0, 60°C | Thermothelomyces thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.4 | carboxymethyl cellulose + H2O | - |
Pseudoalteromonas sp. DY3 | ? | - |
? | |
3.2.1.8 | additional information | the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover | Thermothelomyces thermophilus | ? | - |
? | |
3.2.1.8 | additional information | the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover | Thermothelomyces thermophilus ATCC 42464 | ? | - |
? | |
3.2.1.8 | additional information | the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover | Thermothelomyces thermophilus BCRC 31852 | ? | - |
? | |
3.2.1.8 | additional information | the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover | Thermothelomyces thermophilus DSM 1799 | ? | - |
? | |
3.2.1.8 | xylan + H2O | RBB-xylan as substrate | Thermothelomyces thermophilus | ? | - |
? | |
3.2.1.8 | xylan + H2O | RBB-xylan as substrate | Thermothelomyces thermophilus ATCC 42464 | ? | - |
? | |
3.2.1.8 | xylan + H2O | RBB-xylan as substrate | Thermothelomyces thermophilus BCRC 31852 | ? | - |
? | |
3.2.1.8 | xylan + H2O | RBB-xylan as substrate | Thermothelomyces thermophilus DSM 1799 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.4 | ? | x * 52200, recombinant His-tagged enzyme, SDS-PAGE | Pseudoalteromonas sp. DY3 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.4 | CelX | - |
Pseudoalteromonas sp. DY3 |
3.2.1.4 | endoglucanase | - |
Pseudoalteromonas sp. DY3 |
3.2.1.8 | endo-beta-1, 4-xylanase | - |
Thermothelomyces thermophilus |
3.2.1.8 | MYCTH_49824 | - |
Thermothelomyces thermophilus |
3.2.1.8 | MYCTH_56237 | - |
Thermothelomyces thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 45 | - |
recombinant enzyme | Pseudoalteromonas sp. DY3 |
3.2.1.8 | 60 | - |
recombinant enzyme | Thermothelomyces thermophilus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 5 | 45 | 34.7% of maximal activity at 5°C, maximal activity at 45°C, rapid loss of activity above. The cold adaptation of enzyme CelX is possibly due to the presence of the unusually long linker between the catalytic module and the cellulose-binding domain | Pseudoalteromonas sp. DY3 |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 25 | 55 | purified recombinant enzyme, very stable at 25°C, loss of about 13.2% activity at 35°C after 2 h. The enzyme retains 10.4% activity at 45°C after 2 h, and is completely inactivated at 55°C after 30 min | Pseudoalteromonas sp. DY3 |
3.2.1.8 | 70 | - |
purified recombinant enzyme, 30 min, 60% activity remaining | Thermothelomyces thermophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.4 | 4.2 | - |
carboxymethyl cellulose | pH 5.5, 45°C, recombinant enzyme | Pseudoalteromonas sp. DY3 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 5.5 | - |
recombinant enzyme | Pseudoalteromonas sp. DY3 |
3.2.1.8 | 6 | - |
recombinant enzyme | Thermothelomyces thermophilus |
3.2.1.8 | 7 | - |
recombinant enzyme | Thermothelomyces thermophilus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 5 | 9 | over 76.9% of maximal activity within this range, no activity at pH 4.0 and below, 59.2% and 42.6% of maximal activity at pH 10.0 and pH 11.0 respectively | Pseudoalteromonas sp. DY3 |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.4 | 4 | - |
purified recombinant His-tagged enzyme, inactivation after 1 h | Pseudoalteromonas sp. DY3 |
3.2.1.4 | 5 | 11 | purified recombinant His-tagged enzyme, 120 h, 83.0% activity remaining, 66% at pH 11.0 after 120 h | Pseudoalteromonas sp. DY3 |
3.2.1.8 | 2 | 12 | purified recombinant enzyme, 60 min, room temperature, MYCTH_49824 retains nearly 70% activity | Thermothelomyces thermophilus |
3.2.1.8 | 2 | 12 | purified recombinant enzyme, 60 min, room temperature, MYCTH_56237 retains nearly 70% activity | Thermothelomyces thermophilus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.8 | evolution | the enzyme belongs to the glycosyl hydrolase family 11, GH11 | Thermothelomyces thermophilus |
3.2.1.8 | additional information | multiple template-based enzyme structure homology modeling | Thermothelomyces thermophilus |