Activating Compound | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | - |
Aspergillus fischeri |
Cloned (Comment) | Organism |
---|---|
gene man5P1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of extracellular enzyme in Pichia pastoris strain GS115 | Aspergillus fischeri |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ag+ | - |
Aspergillus fischeri | |
Co2+ | - |
Aspergillus fischeri | |
Cu2+ | - |
Aspergillus fischeri | |
EDTA | - |
Aspergillus fischeri | |
Fe3+ | - |
Aspergillus fischeri | |
K+ | - |
Aspergillus fischeri | |
Li+ | - |
Aspergillus fischeri | |
Mg2+ | - |
Aspergillus fischeri | |
additional information | the purified recombinant enzyme has a strong resistance to SDS and Ag+ and proteases pepsin and trypsin | Aspergillus fischeri | |
Ni2+ | - |
Aspergillus fischeri | |
SDS | - |
Aspergillus fischeri | |
Zn2+ | - |
Aspergillus fischeri |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | recombinant enzyme, Km for locust bean gum is 0.83 ± 0.2 mg/ml, pH 4.0, 80°C | Aspergillus fischeri |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme contains a putative 19-residue signal peptide at the N-terminus | Aspergillus fischeri | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | poor effects by Na+, Ca2+, and Mn2+ | Aspergillus fischeri |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
39500 | - |
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE | Aspergillus fischeri |
40000 | - |
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE | Aspergillus fischeri |
43000 | - |
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE | Aspergillus fischeri |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Aspergillus fischeri | the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides | ? | - |
? | |
additional information | Aspergillus fischeri P1 | the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fischeri | - |
gene man5P1 | - |
Aspergillus fischeri P1 | - |
gene man5P1 | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the enzyme contains two putative N-glycosylation sites and no O-glycosylation site, deglycosylation by endo-beta-N-acetylglucosaminidase H | Aspergillus fischeri |
Purification (Comment) | Organism |
---|---|
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration and anion exchange chromatography | Aspergillus fischeri |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1703 | - |
purified recombinant enzyme, substrate locust bean gum, pH 4.0, 80°C | Aspergillus fischeri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
galactomannan + H2O | different contents of glucose and mannose, overview | Aspergillus fischeri | mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose | product ratio overview | ? | |
guar gum + H2O | - |
Aspergillus fischeri | mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose | product ratio overview | ? | |
locust bean gum + H2O | - |
Aspergillus fischeri | mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose | product ratio overview | ? | |
mannohexaose + H2O | - |
Aspergillus fischeri | ? | - |
? | |
mannopentaose + H2O | - |
Aspergillus fischeri | ? | - |
? | |
mannopentaose + H2O | - |
Aspergillus fischeri P1 | ? | - |
? | |
mannotetraose + H2O | - |
Aspergillus fischeri | ? | - |
? | |
mannotetraose + H2O | - |
Aspergillus fischeri P1 | ? | - |
? | |
mannotriose + H2O | - |
Aspergillus fischeri | ? | - |
? | |
mannotriose + H2O | - |
Aspergillus fischeri P1 | ? | - |
? | |
additional information | the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides | Aspergillus fischeri | ? | - |
? | |
additional information | the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose | Aspergillus fischeri | ? | - |
? | |
additional information | the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides | Aspergillus fischeri P1 | ? | - |
? | |
additional information | the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose | Aspergillus fischeri P1 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE | Aspergillus fischeri |
Synonyms | Comment | Organism |
---|---|---|
Beta-mannanase | - |
Aspergillus fischeri |
Man5P1 | - |
Aspergillus fischeri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
recombinant enzyme | Aspergillus fischeri |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 90 | recombinant enzyme, over 20% of maximal activity within this range | Aspergillus fischeri |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the glycosylation status of the enzyme has no effect on the thermostability | Aspergillus fischeri |
60 | - |
purified recombinant enzyme, 6 h, over 80% activity remaining | Aspergillus fischeri |
70 | - |
purified recombinant enzyme, 80% activity remaining after 1 h, inactivation after 2 h | Aspergillus fischeri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4 | - |
recombinant enzyme | Aspergillus fischeri |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
2 | 9 | recombinant enzyme, over 20% of maximal activity at pH 2.0 and pH 9.0 | Aspergillus fischeri |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
2 | 12 | purified recombinant enzyme, 1 h, over 65% activity remaining | Aspergillus fischeri |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Aspergillus fischeri | sequence calculation | - |
5.93 |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the glycosyl hydrolase family 5, GH5 | Aspergillus fischeri |