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Kinetic Studies of a Coenzyme b12 Dependent Reaction Catalyzed by Glutamate Mutase from <i>Clostridium cochlearium</i>

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Advances in Enzyme Research 2021年第4期9卷 72-90页

作者： Fredrick Edwin Lyatuu Wolfgang buckel Department of Chemistry College of Natural and Applied Sciences University of Dar es Salaam Dar es Salaam Tanzania Laboratorium für Mikrobiologie Fachbereich Biologie Philipps-Universit&auml t Marburg Karl-von-Frisch Stra&szlig e 8 Marburg Germany Max-Planck-Institut für Terrestrische Mikrobiologie Marburg Germany

The coenzyme b12 dependent glutamate mutase is composed of two apoenzyme proteins subunits;S and E2, which while either fused or separate assemble with coenzyme b12 to form an active holoenzyme (E2S2-b12) for cata... 详细信息

br /> The coenzyme B12 dependent glutamate mutase is composed of two apoenzyme proteins subunits;S and E2, which while either fused or separate assemble with coenzyme B12 to form an active holoenzyme (E2S2-B12) for catalyzing the reversible isomerization between (S)-glutamate and (2S, 3S)-3-methylas- partate. In order to assay the activity of glutamate mutase by UV spectrophotometry, this reaction is often coupled with methylaspartase which deaminates (2S, 3S)-3-methylaspartate to form mesaconate (λmax = 240 nm, Ɛb>240b> = 3.8 mM-1·cm-1). The activities of different reconstitutions of glutamate mutase from separate apoenzyme components S and E in varied amounts of coenzyme B12 and adenosylpeptide B12 as cofactors were measured by this assay and used to reveal the binding properties of the cofactor by the Michaelis- Menten Method. The values of Km for coenzyme B12 in due to reconstitutions of holoenzyme in 2, 7 and 14 S: E were determined as;1.12 ± 0.04 μM, 0.7 ± 0.05 μM and 0.52 ± 0.06 μM, respectively, so as those of adenosylpeptide B12;1.07 ± 0.04 μM and 0.35 ± 0.05 μM as obtained from respective 2 and 14 S: E compositions of holoenzyme. Analysis of these kinetics results curiously associates the increasing affinity of cofactors to apoenzyme with increased amount of component S used in reconstituting holoenzyme from separate apoenzyme components and cofactor. Moreover, in these studies a new method for assaying the activity of glutamate mutase was develo

关键词： Coenzyme b12 adenosylpeptide b12 Glutamate Mutase (S)-Glutamate (2S 3S)-3-Methylaspartate Methylasparatase

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