The 108-kDa peptidylglycine α-amidating monooxygenase precursor contains two separable enzymatic activities involved in peptide amidation
Open Access
- 1 September 1990
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 171 (3) , 926-932
- https://doi.org/10.1016/0006-291x(90)90772-f
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of .alpha.-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine .alpha.-amidating monooxygenase in peptide amidationBiochemistry, 1990
- Immunocytochemical and in Situ Hybridization Studies of Peptidylglycine α-Amidating Monooxygenase in Pituitary Gland*Endocrinology, 1990
- Peptidylglycine α-amidating reaction: Evidence for a two-step mechanism involving a stable intermediate at neutral pHBiochemical and Biophysical Research Communications, 1990
- Rat peptidylglycine α-amidating enzyme: The relation between activities at neutral and alkaline pH valuesArchives of Biochemistry and Biophysics, 1989
- Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl‐CoA hydrataseEuropean Journal of Biochemistry, 1989
- Enzymatic peptidyl .alpha.-amidation proceeds through formation of an .alpha.-hydroxyglycine intermediateJournal of the American Chemical Society, 1989
- Peptide α-AmidationAnnual Review of Physiology, 1988
- Biosynthesis of the C-terminal amide in peptide hormonesBioscience Reports, 1987
- Enzyme‐catalysed peptide amidationEuropean Journal of Biochemistry, 1987
- Structure of the Precursor to an Enzyme Mediating COOH-Terminal Amidation in Peptide BiosynthesisMolecular Endocrinology, 1987