Invertebrate aspartyl/asparaginyl β-hydroxylase: Potential modification of endogenous epidermal growth factor-like modules

  • Monkovic D
  • VanDusen W
  • Petroski C
 et al. 
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Abstract

An invertebrate α-ketoglutarate-dependent aspartyl/asparaginyl β-hydroxylase, which posttranslationally hydroxylates specific aspartyl or asparaginyl residues within epidermal growth factor-like modules, was identified, partially purified and characterized. Preparations derived from two insect cell lines catalyzed the hydroxylation of the expected asparaginyl residue within a synthetic epidermal growth factor-like module. This activity was found to be similar to that of the purified mammalian aspartyl/asparaginyl β-hydroxylase with respect to cofactor requirements, stereochemistry and substrate sequence specificity. Furthermore, recombinant human C1r, expressed in an insect cell-derived baculovirus expression system, was also found to be hydroxylated at the expected asparaginyl residue. Thus, these results establish the potential for invertebrate aspartyl/asparaginyl hydroxylation. Since several invertebrate proteins known to be required for proper embryonic development contain a putative consensus sequence that may be required for hydroxylation, the studies presented here provide the basis for further investigations concerned with identifying hydroxylated invertebrate proteins and determining their physiologic function. © 1992.

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Authors

  • Don D. Monkovic

  • William J. VanDusen

  • Christopher J. Petroski

  • Victor M. Garsky

  • Mohinder K. Sardana

  • Peter Zavodszky

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