Numerous posttranslational modifications provide opportunities for the intricate regulation of metabolic enzymes at multiple levels

Steven C. Huber, Shane C. Hardin

Research output: Contribution to journalReview article


The metabolic plasticity displayed by plants during normal development, and in response to environmental fluctuations and stressors, is essential for their growth and survival. The capacity to regulate metabolic enzymes intricately arises in part from posttranslational modifications that can affect enzymatic activity, intracellular localization, protein-protein interactions, and stability. Protein phosphorylation and thiol/disulfide redox modulation are important modifications in plants, and it is likely that O-glycosylation and S-nitrosylation will also emerge as important mechanisms. Recent advances in the field of proteomics, in particular the development of novel and specific chemistries for the detection of a diverse number of modifications, are rapidly expanding our awareness of possible modifications and our understanding of the enzymes whose functions are likely to be regulated posttranslationally.

Original languageEnglish (US)
Pages (from-to)318-322
Number of pages5
JournalCurrent opinion in plant biology
Issue number3
StatePublished - Jun 1 2004



  • ADP-glucose pyrophosphorylase
  • AGPase
  • CDPK
  • Cys12
  • Cysteine12
  • NO
  • NR
  • O-GlcNAc
  • PTM
  • Ser
  • Suc
  • Thr
  • calcium-dependent protein kinase
  • nitrate reductase
  • nitric oxide
  • posttranslational modification
  • serine
  • sucrose
  • threonine
  • β-O-linked N-acetylglucosamine

ASJC Scopus subject areas

  • Plant Science

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