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Literature summary for 4.2.1.84 extracted from

  • Lipowicz, B.; Hanekop, N.; Schmitt, L.; Proksch, P.
    An aeroplysinin-1 specific nitrile hydratase isolated from the marine sponge Aplysina cavernicola (2013), Mar. Drugs, 11, 3046-3067.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.84

Application

Application Comment Organism
synthesis NHases are important for large scale production of acrylamide and nicotinamide Aplysina cavernicola

KM Value [mM]

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

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 [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

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 (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
heterodimer x * 26000 + x * 72000, SDS-PAGE Aplysina cavernicola
More peptide mapping, overview Aplysina cavernicola

Synonyms

Synonyms Comment Organism
NHase
-
 Aplysina cavernicola

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
41
-
-
 Aplysina cavernicola

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
 Aplysina cavernicola

General Information

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