Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces ‘late onset’ hyperammonaemia
- 1 March 1997
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 322 (2) , 625-631
- https://doi.org/10.1042/bj3220625
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Implications for domain switchingProtein Science, 1996
- Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Characterization of the active site and evidence for an interdomain carboxy‐terminal helix in ornithine transcarbamoylaseProtein Science, 1996
- Effects of Assembly and Mutations Outside the Active Site on the Functional pH Dependence of Escherichia coli Aspartate TranscarbamylaseJournal of Biological Chemistry, 1996
- Fluorescence lifetimes of the tryptophan residues in ornithine transcarbamoylaseBiochemistry, 1993
- A novel missense mutation in exon 8 of the ornithine transcarbamylase gene in two unrelated male patients with mild ornithine transcarbamylase deficiencyHuman Genetics, 1991
- Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylaseBiochemistry, 1990
- Zn2+ regulation of ornithine transcarbamoylaseJournal of Molecular Biology, 1990
- Reconstruction of an enzyme by domain substitution effectively switches substrate specificityNature, 1989
- Substrate specificity and protonation state of ornithine transcarbamoylase as determined by pH studiesBiochemistry, 1985
- δ-(phosphonacetyl)-L-ornithine, a potent transition state analogue inhibitor of ornithine carbamoyltransferaseBiochemical and Biophysical Research Communications, 1977