Peptidylglycine alpha-hydroxylating monooxygenase/peptidyl-hydroxyglycine alpha-amidating lyase
Short name | PHM/PAL |
Overlapping homologous superfamilies |
Description
References
1.Characterization of novel mRNAs encoding enzymes involved in peptide alpha-amidation. Stoffers DA, Ouafik L, Eipper BA. J. Biol. Chem. 266, 1701-7, (1991). View articlePMID: 1988445
2.The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains. Ouafik LH, Stoffers DA, Campbell TA, Johnson RC, Bloomquist BT, Mains RE, Eipper BA. Mol. Endocrinol. 6, 1571-84, (1992). View articlePMID: 1448112
Further reading
3. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Prigge ST, Mains RE, Eipper BA, Amzel LM. Cell. Mol. Life Sci. 57, 1236-59, (2000). View articlePMID: 11028916
4. The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation. Klinman JP. J. Biol. Chem. 281, 3013-6, (2006). View articlePMID: 16301310
5. PHM is required for normal developmental transitions and for biosynthesis of secretory peptides in Drosophila. Jiang N, Kolhekar AS, Jacobs PS, Mains RE, Eipper BA, Taghert PH. Dev. Biol. 226, 118-36, (2000). View articlePMID: 10993678
6. Drosophila uses two distinct neuropeptide amidating enzymes, dPAL1 and dPAL2. Han M, Park D, Vanderzalm PJ, Mains RE, Eipper BA, Taghert PH. J. Neurochem. 90, 129-41, (2004). View articlePMID: 15198673
GO terms
biological process
molecular function
cellular component
Cross References
Contributing Member Database Entry
- PRINTS:PR00790