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

Don D. Monkovic, William J. VanDusen, Christopher J. Petroski, Victor M. Garsky, Mohinder K. Sardana, P. Závodszky, Andrew M. Stern, Paul A. Friedman

Research output: Contribution to journalArticle

26 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)233-241
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume189
Issue number1
DOIs
Publication statusPublished - Nov 30 1992

Fingerprint

Invertebrates
Mixed Function Oxygenases
Epidermal Growth Factor
Hydroxylation
Insects
Stereochemistry
Baculoviridae
Consensus Sequence
Substrate Specificity
Embryonic Development
Proteins
Cells
Cell Line
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Invertebrate aspartyl/asparaginyl β-hydroxylase : Potential modification of endogenous epidermal growth factor-like modules. / Monkovic, Don D.; VanDusen, William J.; Petroski, Christopher J.; Garsky, Victor M.; Sardana, Mohinder K.; Závodszky, P.; Stern, Andrew M.; Friedman, Paul A.

In: Biochemical and Biophysical Research Communications, Vol. 189, No. 1, 30.11.1992, p. 233-241.

Research output: Contribution to journalArticle

Monkovic, Don D. ; VanDusen, William J. ; Petroski, Christopher J. ; Garsky, Victor M. ; Sardana, Mohinder K. ; Závodszky, P. ; Stern, Andrew M. ; Friedman, Paul A. / Invertebrate aspartyl/asparaginyl β-hydroxylase : Potential modification of endogenous epidermal growth factor-like modules. In: Biochemical and Biophysical Research Communications. 1992 ; Vol. 189, No. 1. pp. 233-241.
@article{80f66fc8648a40c5bef7afe57f6f2aed,
title = "Invertebrate aspartyl/asparaginyl β-hydroxylase: Potential modification of endogenous epidermal growth factor-like modules",
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.",
author = "Monkovic, {Don D.} and VanDusen, {William J.} and Petroski, {Christopher J.} and Garsky, {Victor M.} and Sardana, {Mohinder K.} and P. Z{\'a}vodszky and Stern, {Andrew M.} and Friedman, {Paul A.}",
year = "1992",
month = "11",
day = "30",
doi = "10.1016/0006-291X(92)91549-6",
language = "English",
volume = "189",
pages = "233--241",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Invertebrate aspartyl/asparaginyl β-hydroxylase

T2 - Potential modification of endogenous epidermal growth factor-like modules

AU - Monkovic, Don D.

AU - VanDusen, William J.

AU - Petroski, Christopher J.

AU - Garsky, Victor M.

AU - Sardana, Mohinder K.

AU - Závodszky, P.

AU - Stern, Andrew M.

AU - Friedman, Paul A.

PY - 1992/11/30

Y1 - 1992/11/30

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027051671&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027051671&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(92)91549-6

DO - 10.1016/0006-291X(92)91549-6

M3 - Article

C2 - 1449478

AN - SCOPUS:0027051671

VL - 189

SP - 233

EP - 241

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -