Large substrates

Fig. 1. Inhibition of porcine pancreatic a-amylase. Substrates, an inhibitor, and their binding orientations in the active site are shown schematically. The arrows denote the catalytic site in each case, (a) The small substrate, G2PNP [17400-77-0] (3) (b) the large substrate, G OH [13532-61 -1] (4) and (c) the inhibitor, 4-phenyl imidazole (5) and the substrate G2PNP (3) in the binding orientation for noncompetitive inhibition. The binding orientation of G2PNP...

The complex structure of the enzyme can show a very large substrate-enzyme interaction specificity, which can be traduced to a high degree of chemo-, regio-, or stereoselectivity. For this reason, nowadays, the versatility of biotransformations for synthetic proposals is an excellent tool for organic chemists [9]. 

Styrene was successfully oxidized to the S-product both by xylene monooxygenase from P. putida mt-2 [113] and styrene monooxygenase from Pseudomonas sp.VLB120 [114] (Scheme 9.13), with the latter enzyme displaying a particularly large substrate tolerance with excellent stereoselectivity (>99% ee). In this context it is interesting to note that both xylene monooxygenase as well as chloroperoxidase are very selective for mono-epoxidation in case of presence of multiple alkene functionalities [115]. 

As indicated in Fig. 1, nitrogenase can reduce substrates other than Na. In the absence of other reducible substrates it will reduce protons to dihydrogen, but it can also reduce a number of other small triple-bonded substrates, as indicated in Section V,E,1. Large substrates are not reduced efficiently, indicating physical limitations on access to the enzyme s active site. CO is a potent inhibitor of all nitrogenase substrate reductions except that of the proton to Ha. In the presence of CO the rate of electron transfer is generally not inhibited, but all electrons go toward the production of Ha. 

The rate effects imposed by this derivative, however, are dependent on the structure of the substrate. For example, the hydrolysis of 8-acetoxy-5-quinoline-sulfonate (AQS), a large substrate which cannot be included within the cyclohexaamylose cavity, is not enhanced by this derivative. Moreover, in contrast to the effects of unmodified cycloamyloses on the hydrolyses of nitrophenyl acetates, the rate accelerations imposed by this... 

The binding of a substrate to its active center was first postulated by E. Fisher in 1894 using the lock and key mechanism which states that the enzyme interacts with its substrate like a lock and a key, respectively, i.e. the substrate has a matching shape to fit into the active site. This theory assumed that the structure of the catalyst was completely rigid and could not explain why the macromolecule was able to catalyze reactions involving large substrates and not those with small ones, or why they could convert non natural compounds with different structural properties to the substrate. 

Separately housed sensors mounted on large substrates - differentiation by different metal oxides... 

D Immobilized substrate where mineral to be removed is bound to a large substrate permitting simple mechanical separation Robotic manipulation... 

When the reactions of alkyl bromides (n-Q-Cg) with phenoxide were carried out in the presence of cosolvent catalyst 51 (n = 1 or 2,17 % RS) under triphase conditions without stirring, rates increased with decreased chain length of the alkyl halide 82). The substrate selectivity between 1-bromobutane and 1-bromooctane approached 60-fold. Lesser selectivity was observed for polymer-supported HMPA analogue 44 (5-fold), whereas the selectivity was only 1,4-fold for polymer-supported phosphonium ion catalyst 1. This large substrate selectivity was suggested to arise from differences in the effective concentration of the substrates at the active sites. In practice, absorption data showed that polymer-supported polyethylene glycol) 51 and HMPA analogues 44 absorbed 1-bromobutane in preference to 1-bromooctane (6-7 % excess), while polymer-supported phosphonium ion catalyst 1 absorbed both bromides to nearly the same extent. 

Vanillyl alcohol oxidase (VAO) is a flavoenzyme from the ascomycete Penicil-lium simplicissimum that converts a broad range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes. This large substrate specificity makes it possible to obtain vanillin from two major pathways. 

Polarization interactions for atoms and small molecules or functional groups are much weaker than the other interactions listed above. For example, in vacuum the attractive energy between two methyl groups is only about 0.15 kcal/mol (0.6 kJ/mol) at a separation of 0.4 nm. However, polarization interactions are additive, so that for large bodies with many individual polarization interactions (e.g., a protein binding a large substrate molecule) the overall contribution may be 10 to 20 kcal/mol (40-80 kJ/mol). Furthermore, these interactions will be present for both nonpolar and polar (even ionic) groups. 

Here we report the synthesis and catalytic application of a new porous clay heterostructure material derived from synthetic saponite as the layered host. Saponite is a tetrahedrally charged smectite clay wherein the aluminum substitutes for silicon in the tetrahedral sheet of the 2 1 layer lattice structure. In alumina - pillared form saponite is an effective solid acid catalyst [8-10], but its catalytic utility is limited in part by a pore structure in the micropore domain. The PCH form of saponite should be much more accessible for large molecule catalysis. Accordingly, Friedel-Crafts alkylation of bulky 2, 4-di-tert-butylphenol (DBP) (molecular size (A) 9.5x6.1x4.4) with cinnamyl alcohol to produce 6,8-di-tert-butyl-2, 3-dihydro[4H] benzopyran (molecular size (A) 13.5x7.9x 4.9) was used as a probe reaction for SAP-PCH. This large substrate reaction also was selected in part because only mesoporous molecular sieves are known to provide the accessible acid sites for catalysis [11]. Conventional zeolites and pillared clays are poor catalysts for this reaction because the reagents cannot readily access the small micropores. 

As was shown in Chapter 11, the binding energy of an enzyme and substrate is potentially very high. However, A s are usually found to be relatively high. An extreme example of this is NAD+. This large substrate has two ribose moieties,... 

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