Peptidylglycine alpha-amidating monooxygenase

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Peptidylglycine alpha-amidating monooxygenase
File:PBB Protein PAM image.jpg
PDB rendering based on 1opm.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PAM ; PAL; PHM
External IDs Template:OMIM5 Template:MGI HomoloGene37369
RNA expression pattern
File:PBB GE PAM 202336 s at tn.png
File:PBB GE PAM 212958 x at tn.png
File:PBB GE PAM 214620 x at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Peptidylglycine alpha-amidating monooxygenase, also known as PAM, is a human gene.[1]

This gene encodes a multifunctional protein. It has two enzymatically active domains with catalytic activities - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These catalytic domains work sequentially to catalyze neuroendocrine peptides to active alpha-amidated products. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene but some of their full length sequences are not yet known.[1]

References

  1. 1.0 1.1 "Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase".

Further reading

  • Pittner RA, Albrandt K, Beaumont K; et al. (1994). "Molecular physiology of amylin". J. Cell. Biochem. 55 Suppl: 19–28. PMID 7929615.
  • Eipper BA, Milgram SL, Husten EJ; et al. (1993). "Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains". Protein Sci. 2 (4): 489–97. PMID 8518727.
  • Ouafik LH, Stoffers DA, Campbell TA; et al. (1992). "The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains". Mol. Endocrinol. 6 (10): 1571–84. PMID 1448112.
  • Maltese JY, Eipper BA (1993). "Developmental expression of peptidylglycine alpha-amidating monooxygenase (PAM) in primary cultures of neonatal rat cardiocytes: a model for studying regulation of PAM expression in the rat heart". Mol. Endocrinol. 6 (12): 1998–2008. PMID 1491686.
  • Braas KM, Harakall SA, Ouafik L; et al. (1992). "Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study". Endocrinology. 130 (5): 2778–88. PMID 1572293.
  • Glauder J, Ragg H, Rauch J, Engels JW (1990). "Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells". Biochem. Biophys. Res. Commun. 169 (2): 551–8. PMID 2357221.
  • Roberts AN, Leighton B, Todd JA; et al. (1990). "Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus". Proc. Natl. Acad. Sci. U.S.A. 86 (24): 9662–6. PMID 2690069.
  • Vos MD, Jones JE, Treston AM (1995). "Human peptidylglycine alpha-amidating monooxygenase transcripts derived by alternative mRNA splicing of an unreported exon". Gene. 163 (2): 307–11. PMID 7590286.
  • Tsukamoto T, Noguchi M, Kayama H; et al. (1995). "Increased peptidylglycine alpha-amidating monooxygenase activity in cerebrospinal fluid of patients with multiple sclerosis". Intern. Med. 34 (4): 229–32. PMID 7606087.
  • Yun HY, Johnson RC, Mains RE, Eipper BA (1993). "Topological switching of the COOH-terminal domain of peptidylglycine alpha-amidating monooxygenase by alternative RNA splicing". Arch. Biochem. Biophys. 301 (1): 77–84. doi:10.1006/abbi.1993.1117. PMID 7680192.
  • Mains RE, Milgram SL, Keutmann HT, Eipper BA (1995). "The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins". Mol. Endocrinol. 9 (1): 3–13. PMID 7760848.
  • Tateishi K, Arakawa F, Misumi Y; et al. (1995). "Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase". Biochem. Biophys. Res. Commun. 205 (1): 282–90. doi:10.1006/bbrc.1994.2662. PMID 7999037.
  • Martínez A, Montuenga LM, Springall DR; et al. (1993). "Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas". J. Histochem. Cytochem. 41 (3): 375–80. PMID 8094086.
  • Kapuscinski M, Green M, Sinha SN; et al. (1993). "Peptide alpha-amidation activity in human plasma: relationship to gastrin processing". Clin. Endocrinol. (Oxf). 39 (1): 51–8. PMID 8102327.
  • Yun HY, Keutmann HT, Eipper BA (1994). "Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase". J. Biol. Chem. 269 (14): 10946–55. PMID 8144680.
  • Ouafik LH, Mattei MG, Giraud P; et al. (1994). "Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21". Genomics. 18 (2): 319–21. PMID 8288234.
  • Husten EJ, Tausk FA, Keutmann HT, Eipper BA (1993). "Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase". J. Biol. Chem. 268 (13): 9709–17. PMID 8486658.
  • Yun HY, Milgram SL, Keutmann HT, Eipper BA (1996). "Phosphorylation of the cytosolic domain of peptidylglycine alpha-amidating monooxygenase". J. Biol. Chem. 270 (50): 30075–83. PMID 8530412.

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