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Article

Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase.

The Journal of biological chemistry - 8 Apr 1994

Yun H Y, Keutmann H T, Eipper B A

Abstract excerpt

Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the COOH-terminal alpha-amidation of neuro-endocrine peptides through the sequential action of monooxygenase and lyase domains contained within this bifunctional protein. Alternative splicing leads to the expression of soluble and integral membrane bifunctional PAM proteins as well as a soluble monofunctional monooxygenase. In order to determine how...

Topics

Alternative Splicing
Animals
Base Sequence
Cells, Cultured
DNA Primers
Humans
Mixed Function Oxygenases
Molecular Sequence Data
Multienzyme Complexes
Mutation
Oligosaccharides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Rats

Subcellular Fractions

Sulfates

Tyrosine

Source

Identifiers

PMID: 8144680

Genes

PAM

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8144680-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase.PMID 8144680Read ↗

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