Stereospecificity of allantoin degradation inStreptococcus allantoicus

Zusammenfassung Die Stereospezifität der Enzyme des Allantoinabbaus inStreptococcus allantoicus und die optische Drehung der Reaktionsprodukte wurde bestimmt. Allantoinase war aspezifisch, während Allantoate-amidohydrolase ausschliesslich (-)-Ureidoglykolate bildete. Diese Substanz wurde durch (-)-Ureidoglykolase hydrolysiert.     

Structure of the actin-myosin interface

The topography of the rigor complex between F-actin and myosin heads (S1) has been investigated by carbodiimide zero-length cross-linking. The results demonstrate for the first time that the 95,000-molecular weight (95K) heavy chain of the myosin head enters into van der Waals contact with two neighbouring actin monomers; one is bound to the 50K domain and the other to the 20K domain of the myosin chain. The covalent F-actin-S1 complex can be isolated; it shows a vastly elevated Mg2+-ATPase. Each pair of actin subunits in the thin filament seems to act as a functional unit for specific binding of a myosin head and stimulation of its Mg2+-ATPase activity.