[Solid-phase enzymatic reactions. V. Comparison of catalytic properties of subtilisin and alpha-chymotrypsin in the absence of a solvent].
Subtilisin Carlsberg (E.C. 3.4.21.14) catalyzes the hydrolysis of N-succinyl-L-phenylalanine p-nitroanilide in solid-state solvent-free hydrated protein-substrate mixtures. This process needs a certain critical degree of hydration of the protein molecule which is attained at the relative water vapour pressure (p/ps) above 0.49. The identical hydration dependency was found for the solid-state inactivation of subtilisin by phenylmethylsulphonylfluoride. Despite the fact that subtilisin and alpha-chymotrypsin belong to two different families of serine proteinases, the characteristics of their solid-state catalytic reactions are almost identical.
Maksareva
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D002384:Catalysis; D002918:Chymotrypsin / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007124:Immunoenzyme Techniques; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D012997:Solvents; D013381:Subtilisins / Q000378:metabolism*; D014867:Water
D015842:Serine Proteinase Inhibitors; D012997:Solvents; D014867:Water; C011358:Suphepa; D010649:Phenylalanine; D013381:Subtilisins; D002918:Chymotrypsin