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• W1565432362 abstract "Upon resolution of the particulate cell fraction of Veilionella aclcalescens by chromatography, membranes and ribosomes were celarly resolved. Methylmalony‐CoA decarboxylase was bound to the membranes and not to ribosomes as reported earler. Membrane vesicels containing mentylmalonyl‐CoA decarboxylase were prepared by disrupting V. alcalescens cells with French pressure chdmaber. About 64% of the decaroxylase was oriented in these vesicles with the sbstrated binding site facing to the outside. The vesicels perforemd a rapid acdumulation of Na + ions in respon se to the decarboylatino of methylmalonyl‐CoA.Decarbosylation and transport wer highly uncouped. The effciency of the transport was considerably increased if methylmalonyl‐CoA cecarbosylation was retared by using a low temperature of by slowaly genrating the substrate enzymically form priopionyl‐CoA. Under optimized coditions Na + was concentrated inside the inverted vesicles eight‐times than in the incuabaion medium. Mehtylmalonyl‐CoA decarboxylase was solubilized formt eh membranes with Tritom X‐100 and purified about 20‐fp;d nu affinity chromatography on monomeric avidin‐Sepharose coulmns. The decarboxylase was specifically activated by Na + ions (apparend K m ∼ 0.6 mM). Wherase ( S )‐methylmalonyl‐CoA was the superior substrte. (apparent k m ∼ 7 μM). The decarboxylation of methylmalonyl‐CoA yielded CO 2 and not HCO 3 − as th primary reaction product. Analysis of the prurified enzyme by dodecylsulfate gel electrophoresis inducated the presence of four differnet polypetides α, β, γ, δ with M r 60 0000, 33 0000, 18 500 and 14000. The letter of these polypetides was elearly visible only after stiaing but not after staining with Coomassie brilliant blue. A low moleualr weight polypetide wit similar staaining properties also found in oxaloacetate decarbvoxylase Methylmalonyl‐CoA decarboxlase contained about 1 mol convalently bound biotin per 125 500 g protien which was localized exculsively in the γ‐subunit. This subunit therfore represents th biotin carboysl carier protein of methylmalonyl‐CoA decarboxylase. A new very senstivitymethod for the dtection of biotin containg proteins is described." @default.
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• W1565432362 date "1983-05-01" @default.
• W1565432362 modified "2023-10-03" @default.
• W1565432362 title "Purification and Characterization of a New Sodium-Transport Decarboxylase. Methytlaomyl-CoA Decarboxylase from Veillonella alcalescens" @default.
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• W1565432362 doi "https://doi.org/10.1111/j.1432-1033.1983.tb07403.x" @default.
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