Peptidylglycine alpha-amidating monooxygenase

Peptidylglycine alpha-amidating monooxygenase
Peptidylglycine alpha-amidating monooxygenase

PDB rendering based on 1opm.
Identifiers
Symbols PAM; PAL; PHM
External IDs OMIM170270 MGI97475 HomoloGene37369 GeneCards: PAM Gene
RNA expression pattern
PBB GE PAM 202336 s at tn.png
PBB GE PAM 212958 x at tn.png
PBB GE PAM 214620 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5066 18484
Ensembl ENSG00000145730 ENSMUSG00000026335
UniProt P19021 Q8BQ31
RefSeq (mRNA) NM_000919.3 NM_013626.3
RefSeq (protein) NP_000910.2 NP_038654.2
Location (UCSC) Chr 5:
102.09 – 102.37 Mb
Chr 1:
99.69 – 99.99 Mb
PubMed search [1] [2]

Peptidyl-glycine alpha-amidating monooxygenase is an enzyme that in humans is encoded by the PAM gene.[1][2]

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.[2]

Interactions

Peptidylglycine alpha-amidating monooxygenase has been shown to interact with TSC2.[3]

References

  1. ^ Glauder J, Ragg H, Rauch J, Engels JW (Jul 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. doi:10.1016/0006-291X(90)90366-U. PMID 2357221. 
  2. ^ a b "Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5066. 
  3. ^ Murthy, Vanishree; Han Sangyeul, Beauchamp Roberta L, Smith Nicole, Haddad Luciana A, Ito Naoto, Ramesh Vijaya (Jan. 2004). "Pam and its ortholog highwire interact with and may negatively regulate the TSC1.TSC2 complex". J. Biol. Chem. (United States) 279 (2): 1351–8. doi:10.1074/jbc.M310208200. ISSN 0021-9258. PMID 14559897. 

Further reading




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