mesaconase activity of class I fumarase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase
mesaconase activity of class I fumarase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase
constitutive enzyme, the enzyme may play a role in the interconversion between S-malate and fumarate in addition to that between S-citramalate and mesaconate
mesaconase activity of class I fumarase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase
mesaconase activity of class I fumarase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase
constitutive enzyme, the enzyme may play a role in the interconversion between S-malate and fumarate in addition to that between S-citramalate and mesaconate
mesaconase activity of the promiscuous fumarase/mesaconase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase
the enzyme participates in the methylaspartate pathway of glutamate fermentation as well as in the metabolism of various C5-dicarboxylic acids such as mesaconate or L-threo-beta-methylmalate. fumD is clustered with the key genes for two enzymes of the methylaspartate pathway of glutamate fermentation, glutamate mutase and methylaspartate ammonia lyase, converting glutamate to mesaconate
mesaconase activity of the promiscuous fumarase/mesaconase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase
the enzyme participates in the methylaspartate pathway of glutamate fermentation as well as in the metabolism of various C5-dicarboxylic acids such as mesaconate or L-threo-beta-methylmalate. fumD is clustered with the key genes for two enzymes of the methylaspartate pathway of glutamate fermentation, glutamate mutase and methylaspartate ammonia lyase, converting glutamate to mesaconate
the enzyme participates in the methylaspartate pathway of glutamate fermentation as well as in the metabolism of various C5-dicarboxylic acids such as mesaconate or L-threo-beta-methylmalate. fumD is clustered with the key genes for two enzymes of the methylaspartate pathway of glutamate fermentation, glutamate mutase and methylaspartate ammonia lyase, converting glutamate to mesaconate
the enzyme (Bxe_A3136) is in fact a promiscuous fumarase/mesaconase. It has similar efficiencies (kcat/Km) for both fumarate and mesaconate hydration. This promiscuity is physiologically relevant, as it allows the growth of this bacterium on mesaconate as a sole carbon and energy source
the enzyme (Bxe_A3136) is in fact a promiscuous fumarase/mesaconase. It has similar efficiencies (kcat/Km) for both fumarate and mesaconate hydration. This promiscuity is physiologically relevant, as it allows the growth of this bacterium on mesaconate as a sole carbon and energy source
enzyme consists of 2 components, neither component alone possesses hydrolase activity, MW of component I: 46000 Da, gel filtration, MW of component I: 310000 Da, gel filtration, 8 * 37000, SDS-PAGE
the enzyme consists of two components: component I has MW 45000 and component II has MW 310000, determined by gel filtration. A combination of both components gives the active enzyme. At pH 7.5 or below component II partially dissociates into species with molecular weights of about 165000, 82000, and 37000. At pH 9.0 these species reassociate to form active component II of about the original MW. The observed species may represent a monomer, dimer, tetramer and octamer of a single subunit
the enzyme consists of two components: component I has MW 45000 and component II has MW 310000, determined by gel filtration. A combination of both components gives the active enzyme. At pH 7.5 or below component II partially dissociates into species with molecular weights of about 165000, 82000, and 37000. At pH 9.0 these species reassociate to form active component II of about the original MW. The observed species may represent a monomer, dimer, tetramer and octamer of a single subunit
enzyme consists of 2 components, neither component alone possesses hydrolase activity, MW of component I: 46000 Da, gel filtration, MW of component I: 310000 Da, gel filtration, 8 * 37000, SDS-PAGE
at pH 7.5 or below component II partially dissociates into species with molecular weights of about 165000 Da, 82000 Da, and 37000 Da. At pH 9.0 these species reassociate to form active component II of about the original MW. The observed species may represent a monomer, dimer, tetramer and octamer of a single subunit
inactivation by oxygen. Reactivation by incubating the two protein components with a reducing agent and Fe2+ in absence of oxygen. Mn2+ inhibits activation. Effect of temperature and pH on activation
the enzyme is oxygen sensitive, and the aerobically measured activity of the (aerobically) purified protein is relatively low. The incubation of the enzyme with Fe2+ and thiol and following measurement of the activity under strictly anaerobic conditions leads to an 4fold increase in fumarate hydratase activity