Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | 2 mM, 21% inhibition | Aspergillus giganteus | |
EDTA | 2 mM, 14% inhibition | Aspergillus giganteus | |
iodoacetic acid | 2 mM, 25% inhibition | Aspergillus giganteus | |
PMSF | 2 mM, 33% inhibition | Aspergillus giganteus | |
SDS | 2 mM, 94% inhibition | Aspergillus giganteus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km for citrus pectin with methylation degree of the carboxyl groups of pectin: 4.9 mg/ml. Km for citrus pectin with methylation degree of the carboxyl groups of pectin: 4.6 mg/ml | Aspergillus giganteus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | 2 mM, 1.32fold activation | Aspergillus giganteus | |
Ca2+ | 2 mM, 1.07fold activation | Aspergillus giganteus | |
Co2+ | the enzyme is stimulated by divalent cations, with Co2+ having the strongest effect. 2 mM, 1.54fold activation | Aspergillus giganteus | |
Mg2+ | 2 mM, 1.26fold activation | Aspergillus giganteus | |
NaCl | 2 mM, 1.1fold activation | Aspergillus giganteus | |
Pb2+ | 2 mM, 1.35fold activation | Aspergillus giganteus | |
Zn2+ | 2 mM, 1.17fold activation | Aspergillus giganteus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
63000 | - |
gel filtration | Aspergillus giganteus |
71000 | - |
SDS-PAGE | Aspergillus giganteus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus giganteus | - |
- |
- |
Aspergillus giganteus CCT 3232 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Aspergillus giganteus |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1,4-alpha-D-galacturonosyl methyl ester)n | the enzyme acts on the non-reducing end of methyl-esterified polygalacturonan, releasing either 4-deoxy-L-threo-hex-4-enopyranuronate or 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate. It is able to act on substrates as short as a disaccharide, and is active on substrates with degrees of methyl esterification ranging between 34% and 90%. The enzyme is able to digest apple pectin and citrus pectins with different degrees of methyl esterification | Aspergillus giganteus | (1,4-alpha-D-galacturonosyl methyl ester)n-1 + 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate | - |
? | |
(1,4-alpha-D-galacturonosyl methyl ester)n | the enzyme acts on the non-reducing end of methyl-esterified polygalacturonan, releasing either 4-deoxy-L-threo-hex-4-enopyranuronate or 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate. It is able to act on substrates as short as a disaccharide, and is active on substrates with degrees of methyl esterification ranging between 34% and 90%. The enzyme is able to digest apple pectin and citrus pectins with different degrees of methyl esterification | Aspergillus giganteus CCT 3232 | (1,4-alpha-D-galacturonosyl methyl ester)n-1 + 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
exo-pectin lyase | - |
Aspergillus giganteus |
PLIII | - |
Aspergillus giganteus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Aspergillus giganteus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | 60 | 35°C: about 50% of maximal activity, 60°C: about 45% of maximal activity | Aspergillus giganteus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
15 min,in the absence of substrate, 30% loss of activity | Aspergillus giganteus |
50 | - |
half-life: 9 min | Aspergillus giganteus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
- |
Aspergillus giganteus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 9 | pH 7.0: about 45% of maximal activity, pH 9.0: about 55% of maximal activity | Aspergillus giganteus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3 | 7 | 4°C, 24 h, the enzyme solutions keeps more than 90% lyase activity after 24 h | Aspergillus giganteus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | the enzyme binds an NAD+ cofactor | Aspergillus giganteus |