Structure determinants and substrate recognition of serine carboxypeptidase-like acyltransferases from plant secondary metabolism.

@article{Stehle2006StructureDA,
  title={Structure determinants and substrate recognition of serine carboxypeptidase-like acyltransferases from plant secondary metabolism.},
  author={Felix Stehle and Wolfgang Brandt and Carsten Milkowski and D ieter Strack},
  journal={FEBS letters},
  year={2006},
  volume={580 27},
  pages={6366-74}
}
Structures of the serine carboxypeptidase-like enzymes 1-O-sinapoyl-beta-glucose:L-malate sinapoyltransferase (SMT) and 1-O-sinapoyl-beta-glucose:choline sinapoyltransferase (SCT) were modeled to gain insight into determinants of specificity and substrate recognition. The structures reveal the alpha/beta-hydrolase fold as scaffold for the catalytic triad Ser-His-Asp. The recombinant mutants of SMT Ser173Ala and His411Ala were inactive, whereas Asp358Ala displayed residual activity of 20%. 1-O… CONTINUE READING

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