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Mapping the Limits of Substrate Specificity of the Adenylation Domain of TycA by Benoit R. M. Villiers; Florian Hollfelder is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The limits and potential of substrate promiscuity of the adenylation domain of tyrocidine synthetase 1 were systematically explored. Substrate acceptance is governed by hydrophobic effects (as shown by the correlation of __k__~cat~/__K__~M~ and side‐chain log __P__), shape complementarity and steric exclusion. The quantification of these factors provides ground rules for understanding and possibly evolving substrate specificity in this class of enzymes.magnified image The catalytic potential of tyrocidine synthetase 1 (TycA) was probed by the kinetic characterization of its adenylation activity. We observed reactions with 30 substrates, thus suggesting some substrate promiscuity. However, although the TycA adenylation (A) domain was able to accommodate alternative substrates, their __k__~cat~/__K__~M~ values ranged over six orders of magnitude. A comparison of the activities allowed the systematic mapping of the substrate specificity determinants of the TycA A‐domain. Hydrophobicity plays a major role in the recognition of substrate analogues but can be combined with shape complementarity, conferring higher activity, and/or steric exclusion, leading to substantial discr

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Author

Benoit R. M. Villiers; Florian Hollfelder

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley (ISSN 1439-4227)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)