The Acid-Base Catalytic Machinery

The acid-base catalytic machinery shows slight variations within families. Thus, the active site glutamate in the GH 3 p-glucosidase labelled by A-bromoacetylglucosylamine is not strictly conserved in GH 3, and there individual members of GH 1 and GH 2 which have difierent acid or base catalysts than the majority. 

---

The results of a computational study revealed that the sedolisins, a family of ser-inecarboxyl peptidases, may evoke different catalytic machineries than do classical serine proteases in achieving transition-state stabilization. The family is characterized by a unique catalytic triad, Ser-Glu-Asp, that operates primarily through a general acid-base mechanism.76... 

Mechanisms of Serine Hydrolases. Typical to enzymatic reactions, the enzyme (E) first binds its substrate (S) at the active site as an enzyme-substrate complex (E S). For the formation of the product P, the enzyme-catalyzed reaction then takes place through the mechanism typical of the enzyme. At the active site of serine hydrolases (lipases, carboxylesterases, and serine proteases), the catalytic machinery is called a cataljdic triad consisting of amino acid residues Ser, His, and either Asp or Glu (Fig. 5). In the E S complex, imidazole of His serves as a general acid/base catalyst, catalyzing the addition of the alcoholic hydroxyl of the serine residue to the carbonyl carbon of the acyl donor (R C02R, the first substrate S ). This leads both to the liberation of the first product P (R OH) and to the formation of the so-called acyl-enzyme intermediate. This ester intermediate then reacts with the second substrate (R OH), which leads to the... 

Very recently, lactones have received increasing attention as potential renewable platform chemicals. Perhaps the most prominent bio-based hydroxy fatty acids lactic acid, whose cyclic ester of two lactate molecules serves precursor for the synthesis of bio-based polymers. Fermentative production of hydroxyl-carboxylic acids from agro-industrial waste is an alternative to the synthesis from dwindling fossil resources (Fiichtenbusch et al. 2000). The enzymatic machinery for the production of polyhydroxyalkanoates (PHA) in bacteria offers catalytic pathways for the production of these lactone precursors (Efe et al. 2008). Recent examples include the microbial synthesis of y-butyrolactone and y-valerolactone. Particularly y-valerolactone is of importance and ranks among the top key components of the biomass-based economy. Microbial processes thus offer the perspective of a sustainable fermentative production of optically pure renewable lactones. 

---