Application | Comment | Organism |
---|---|---|
synthesis | NHases are important for large scale production of acrylamide and nicotinamide | Aplysina cavernicola |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the enzymatic in vitro enzyme assay Michaelis-Menten kinetics does not give satisfactory results both for Km and for Vmax as saturation of the enzyme is not reached before the substrate aeroplysinin-1 precipitated at concentrations higher than 36 mM | Aplysina cavernicola |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it | Aplysina cavernicola | |
Mn2+ | the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it. One site binding model with Km = 0.8 mM | Aplysina cavernicola | |
additional information | no activity with Fe2+ | Aplysina cavernicola | |
Ni2+ | the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it | Aplysina cavernicola |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
26000 | - |
x * 26000 + x * 72000, SDS-PAGE | Aplysina cavernicola |
72000 | - |
x * 26000 + x * 72000, SDS-PAGE | Aplysina cavernicola |
146000 | - |
enzyme 2 | Aplysina cavernicola |
242000 | - |
enzyme 1 | Aplysina cavernicola |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aplysina cavernicola | - |
contain at least two NHases, it is currently not known whether the aeroplysinin-1-hydrating enzyme is of sponge origin or produced by its symbiotic microorganisms | - |
Purification (Comment) | Organism |
---|---|
native enzyme 52fold by ultracentrifugation and ammonium sulfate fractionation of the supernatant, followed by ion exchange chromatography and gel filtration | Aplysina cavernicola |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
16.2 | - |
purified native enzyme, pH 7.8, 41°C | Aplysina cavernicola |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
aeroplysinin-1 + H2O | high substrate specificity towards the physiological substrate aeroplysinin-1 | Aplysina cavernicola | verongiaquinol | - |
? | |
additional information | no activity with aeroplysinin-1 derivatives (1S,2R)-3,5-dibromo-1-(cyanomethyl)-4-methoxycyclohexa-3,5-diene-1,2-diyl diacetate, (2-hydroxy-4-methoxyphenyl)acetonitrile, and (3,5-dibromo-2-hydroxy-4-methoxyphenyl)acetonitrile | Aplysina cavernicola | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | x * 26000 + x * 72000, SDS-PAGE | Aplysina cavernicola |
More | peptide mapping, overview | Aplysina cavernicola |
Synonyms | Comment | Organism |
---|---|---|
NHase | - |
Aplysina cavernicola |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
41 | - |
- |
Aplysina cavernicola |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
- |
Aplysina cavernicola |
General Information | Comment | Organism |
---|---|---|
evolution | mass spectrometry of the primary structure of the studied NHases does not reveal any homology to known NHases | Aplysina cavernicola |
physiological function | formation of aeroplysinin-1 and of the corresponding dienone amide is part of the chemical defence system of the mediterrenean sponge Aplysina cavernicola | Aplysina cavernicola |