Candida binding sites

The native form of enzyme in mammalian liver and kidney is a tet-ramer of four identical subunits having molecular weights386,387 35,000. The existence, per enzyme molecule, of four substrate-binding sites and four allosteric sites for the inhibitor AMP has been demonstrated.388-390 On the other hand, the enzyme of Candida utilis has a molecular weight of 100,000, and contains only two subunits.380... 

Figure 14.3 Representation of Candida antarctica B complexed with a covalently bound phosphonate ligand, (a) Ribbon rendering of the protein with the putative lid (red) in the open configuration and the ligand binding site (blue mesh). The mobile regions are shown in red (a5-helix) and yellow (alO-helix). (b) dose up view of the...

Inhibition of lipases, both by the substrate or the product, has been observed. In alcoholysis of methyl propanoate with n-propanol catalyzed by Candida antarctica lipase B (CALB), the alcohol was found to inhibit the enzyme resulting in a deadend complex [21]. Phosphate- and phosphonate-conlaining inhibitors are known to inhibit proteases. Studies of the inhibition of CALB have shown inhibition by diethyl p-nitrophenyl phosphate. The inactivation of the enzyme was caused by covalent binding of diethyl p-nitrophenyl phosphate in the active site [22]. 

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