Front Matter

(Tina Sui) #1
in stereoselectivity result from residues which do not directly contact the substrate,

but have an indirect impact on the binding of triradylglycerols into the substrate

binding site.

Indirect, long-ranging effects are playing a role in all cases where residues far

away from the binding site mediate substrate recognition. They interact either by

changing the structure of the lipase and thus the shape of the binding site, by chan-

ging the physico-chemical properties of the protein, by changing its dynamics and

the flexibility of the binding site, or via long-range electrostatic interactions with the

substrate. While the role of residues directly interacting with substrate are fairly well

understood, the role of more distant residues is mostly obscure. Despite the successes

in engineering substrate binding sites, folding of a protein and the contribution of

individual residues to overall structure and dynamics remains an open question.

5.5 References


Adlercreutz, P. (1991), On the importance of the support material for enzymatic synthesis in organic
media. Support effects at controlled water activity.,Eur. J. Biochem 199 , 609–614.
Atomi, H., Bornscheuer, U., Soumanou, M.M., Beer, H.D., Wohlfahrt, G., Schmid, R.D. (1996),Oils-
Fats-Lipids, 21st World Congress Int. Soc. Fat. Res., P.J. Barnes, Bridgewater, pp. 49–50.
Beer, H.D., Wohlfahrt, G., McCarthy, J.E., Schomburg, D., Schmid, R.D.(1996), Analysis of the catalytic
mechanism of a fungal lipase using computer-aided design and structural mutants,Protein Eng. 9 ,
507–517.


96 5 Molecular Basis of Specificity and Stereoselectivity of Microbial Lipases

Figure 6. Ester substrate insn-1 orientation inRhizopus oryzaelipase (ROL, light gray) andRhizo-
mucor mieheilipase (RML, dark gray) (Scheib et al., 1999). The position of the G266 varies in both lipases
(Ca–Cadistance¼1.3 A ̊) due to the different position of E265 in ROL and T265 in RML, respectively
(horizontal arrow). Therefore, in ROL, the substrate binds deeper into the binding site than in RML
(C2RML–C2ROL¼0.9 A ̊). Hence, steric interactions between thesn-2 substituent and L258 are more
pronounced in ROL rather than RML (vertical arrow). (See color plate, page XVIII).

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