Peptidylglycine alpha-amidating monooxygenase: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Peptidyl-glycine alpha-amidating monooxygenase''' is an [[enzyme]] that is required for the biosynthesis of many signaling peptides.  This transformation is achieved by conversion of a prohormone to the corresponding amide (C(O)NH<sub>2</sub>).  This enzyme is the only known pathway for generating peptide amides, which renders the peptide more hydrophilic.<ref>{{cite journal | vauthors = Eipper BA, Milgram SL, Husten EJ, Yun HY, Mains RE | title = Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains. | journal = Protein Sci. | volume = 2 | issue = 4 | pages = 489–97 | year = 1993 | pmid = 8518727 | pmc = 2142366 | doi = 10.1002/pro.5560020401 }}</ref>  In humans, PAM is encoded by the ''[[PAM (gene)|PAM]]'' [[gene]].<ref name="pmid2357221">{{cite journal | vauthors = Glauder J, Ragg H, Rauch J, Engels JW | title = Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells | journal = Biochem Biophys Res Commun | volume = 169 | issue = 2 | pages = 551–8 | date = Jul 1990 | pmid = 2357221 | pmc =  | doi = 10.1016/0006-291X(90)90366-U }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5066| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
This gene encodes a multifunctional protein. It has two enzymatically active domains with [[Catalytic activity|catalytic activities]] - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These [[catalytic domain]]s work sequentially to catalyze [[neuroendocrine]] [[peptide]]s to active alpha-amidated products. Multiple alternatively spliced transcript variants encoding different [[isoform]]s have been described for this gene, but some of their full-length sequences are not yet known.<ref name="entrez"/>
| image = PBB_Protein_PAM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1opm.
| PDB = {{PDB2|1opm}}, {{PDB2|1phm}}, {{PDB2|1sdw}}, {{PDB2|1yi9}}, {{PDB2|1yip}}, {{PDB2|1yjk}}, {{PDB2|1yjl}}, {{PDB2|3phm}}
| Name = Peptidylglycine alpha-amidating monooxygenase
| HGNCid = 8596
| Symbol = PAM
| AltSymbols =; PAL; PHM
| OMIM = 170270
| ECnumber = 
| Homologene = 37369
| MGIid = 97475
| GeneAtlas_image1 = PBB_GE_PAM_202336_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PAM_212958_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PAM_214620_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004504 |text = peptidylglycine monooxygenase activity}} {{GNF_GO|id=GO:0004598 |text = peptidylamidoglycolate lyase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0031418 |text = L-ascorbic acid binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000790 |text = nuclear chromatin}} {{GNF_GO|id=GO:0000793 |text = condensed chromosome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030141 |text = secretory granule}}
| Process = {{GNF_GO|id=GO:0001519 |text = peptide amidation}} {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006518 |text = peptide metabolic process}} {{GNF_GO|id=GO:0007076 |text = mitotic chromosome condensation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5066
    | Hs_Ensembl = ENSG00000145730
    | Hs_RefseqProtein = NP_000910
    | Hs_RefseqmRNA = NM_000919
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 102229422
    | Hs_GenLoc_end = 102394708
    | Hs_Uniprot = P19021
    | Mm_EntrezGene = 18484
    | Mm_Ensembl = ENSMUSG00000026335
    | Mm_RefseqmRNA = NM_013626
    | Mm_RefseqProtein = NP_038654
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 99651500
    | Mm_GenLoc_end = 99925919
    | Mm_Uniprot = Q8BQ31
  }}
}}
'''Peptidylglycine alpha-amidating monooxygenase''', also known as '''PAM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5066| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
The PHM subunit effects hydroxylation of an O-terminal glycine residue:
{{PBB_Summary
:peptide-C(O)NHCH<sub>2</sub>CO<sub>2</sub><sup>−</sup>  + O<sub>2</sub> +  2 [H]  →  peptide-C(O)NHCH(OH)CO<sub>2</sub><sup>−</sup>  +  H<sub>2</sub>O
| section_title =
Involving hydroxylation of a hydrocarbon by O<sub>2</sub>, this process relies on a [[copper]] cofactor.  [[Dopamine beta-hydroxylase]], also a copper-containing enzyme, effects a similar transformation.
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5066| accessdate = }}</ref>
}}


==References==
The PAL subunit then completes the conversion, by catalyzing elimination from the hydroxylated glycine:
{{reflist|2}}
:peptide-C(O)NHCH(OH)CO<sub>2</sub><sup>−</sup>  →  peptide-C(O)NH<sub>2</sub> +  CH(O)CO<sub>2</sub><sup>−</sup>
==Further reading==
The eliminated coproduct is [[glyoxylate]], written above as CH(O)CO<sub>2</sub><sup>−</sup>.
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Pittner RA, Albrandt K, Beaumont K, Gaeta LS, Koda JE, Moore CX, Rittenhouse J, Rink TJ | title = Molecular physiology of amylin. | journal = J. Cell. Biochem. | volume = 55 Suppl | issue = S1994A | pages = 19–28 | year = 1994 | pmid = 7929615 | doi = 10.1002/jcb.240550004 }}
| citations =
* {{cite journal | vauthors = Ouafik LH, Stoffers DA, Campbell TA, Johnson RC, Bloomquist BT, Mains RE, Eipper BA | title = The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains. | journal = Mol. Endocrinol. | volume = 6 | issue = 10 | pages = 1571–84 | year = 1992 | pmid = 1448112 | doi = 10.1210/me.6.10.1571 }}
*{{cite journal | author=Pittner RA, Albrandt K, Beaumont K, ''et al.'' |title=Molecular physiology of amylin. |journal=J. Cell. Biochem. |volume=55 Suppl |issue= |pages= 19-28 |year= 1994 |pmid= 7929615 |doi= }}
* {{cite journal | vauthors = Maltese JY, Eipper BA | title = 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. | journal = Mol. Endocrinol. | volume = 6 | issue = 12 | pages = 1998–2008 | year = 1993 | pmid = 1491686 | doi = 10.1210/me.6.12.1998 }}
*{{cite journal  | author=Eipper BA, Milgram SL, Husten EJ, ''et al.'' |title=Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains. |journal=Protein Sci. |volume=2 |issue= 4 |pages= 489-97 |year= 1993 |pmid= 8518727 |doi=  }}
* {{cite journal | vauthors = Braas KM, Harakall SA, Ouafik L, Eipper BA, May V | title = Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study. | journal = Endocrinology | volume = 130 | issue = 5 | pages = 2778–88 | year = 1992 | pmid = 1572293 | doi = 10.1210/en.130.5.2778 }}
*{{cite journal | author=Ouafik LH, Stoffers DA, Campbell TA, ''et al.'' |title=The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains. |journal=Mol. Endocrinol. |volume=6 |issue= 10 |pages= 1571-84 |year= 1992 |pmid= 1448112 |doi= }}
* {{cite journal | vauthors = Roberts AN, Leighton B, Todd JA, Cockburn D, Schofield PN, Sutton R, Holt S, Boyd Y, Day AJ, Foot EA | title = Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 24 | pages = 9662–6 | year = 1990 | pmid = 2690069 | pmc = 298561 | doi = 10.1073/pnas.86.24.9662 }}
*{{cite journal | author=Maltese JY, Eipper BA |title=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. |journal=Mol. Endocrinol. |volume=6 |issue= 12 |pages= 1998-2008 |year= 1993 |pmid= 1491686 |doi= }}
* {{cite journal | vauthors = Vos MD, Jones JE, Treston AM | title = Human peptidylglycine alpha-amidating monooxygenase transcripts derived by alternative mRNA splicing of an unreported exon. | journal = Gene | volume = 163 | issue = 2 | pages = 307–11 | year = 1995 | pmid = 7590286 | doi = 10.1016/0378-1119(95)00364-C }}
*{{cite journal | author=Braas KM, Harakall SA, Ouafik L, ''et al.'' |title=Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study. |journal=Endocrinology |volume=130 |issue= 5 |pages= 2778-88 |year= 1992 |pmid= 1572293 |doi= }}
* {{cite journal | vauthors = Tsukamoto T, Noguchi M, Kayama H, Watanabe T, Asoh T, Yamamoto T | title = Increased peptidylglycine alpha-amidating monooxygenase activity in cerebrospinal fluid of patients with multiple sclerosis. | journal = Intern. Med. | volume = 34 | issue = 4 | pages = 229–32 | year = 1995 | pmid = 7606087 | doi = 10.2169/internalmedicine.34.229 }}
*{{cite journal  | author=Glauder J, Ragg H, Rauch J, Engels JW |title=Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells. |journal=Biochem. Biophys. Res. Commun. |volume=169 |issue= 2 |pages= 551-8 |year= 1990 |pmid= 2357221 |doi=  }}
* {{cite journal | vauthors = Yun HY, Johnson RC, Mains RE, Eipper BA | title = Topological switching of the COOH-terminal domain of peptidylglycine alpha-amidating monooxygenase by alternative RNA splicing. | journal = Arch. Biochem. Biophys. | volume = 301 | issue = 1 | pages = 77–84 | year = 1993 | pmid = 7680192 | doi = 10.1006/abbi.1993.1117 }}
*{{cite journal | author=Roberts AN, Leighton B, Todd JA, ''et al.'' |title=Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 24 |pages= 9662-6 |year= 1990 |pmid= 2690069 |doi= }}
* {{cite journal | vauthors = Mains RE, Milgram SL, Keutmann HT, Eipper BA | title = The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins. | journal = Mol. Endocrinol. | volume = 9 | issue = 1 | pages = 3–13 | year = 1995 | pmid = 7760848 | doi = 10.1210/me.9.1.3 }}
*{{cite journal | author=Vos MD, Jones JE, Treston AM |title=Human peptidylglycine alpha-amidating monooxygenase transcripts derived by alternative mRNA splicing of an unreported exon. |journal=Gene |volume=163 |issue= 2 |pages= 307-11 |year= 1995 |pmid= 7590286 |doi= }}
* {{cite journal | vauthors = Tateishi K, Arakawa F, Misumi Y, Treston AM, Vos M, Matsuoka Y | title = Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. | journal = Biochem. Biophys. Res. Commun. | volume = 205 | issue = 1 | pages = 282–90 | year = 1995 | pmid = 7999037 | doi = 10.1006/bbrc.1994.2662 }}
*{{cite journal | author=Tsukamoto T, Noguchi M, Kayama H, ''et al.'' |title=Increased peptidylglycine alpha-amidating monooxygenase activity in cerebrospinal fluid of patients with multiple sclerosis. |journal=Intern. Med. |volume=34 |issue= 4 |pages= 229-32 |year= 1995 |pmid= 7606087 |doi= }}
* {{cite journal | vauthors = Martínez A, Montuenga LM, Springall DR, Treston A, Cuttitta F, Polak JM | title = Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas. | journal = J. Histochem. Cytochem. | volume = 41 | issue = 3 | pages = 375–80 | year = 1993 | pmid = 8094086 | doi = 10.1177/41.3.8094086 }}
*{{cite journal | author=Yun HY, Johnson RC, Mains RE, Eipper BA |title=Topological switching of the COOH-terminal domain of peptidylglycine alpha-amidating monooxygenase by alternative RNA splicing. |journal=Arch. Biochem. Biophys. |volume=301 |issue= 1 |pages= 77-84 |year= 1993 |pmid= 7680192 |doi= 10.1006/abbi.1993.1117 }}
* {{cite journal | vauthors = Kapuscinski M, Green M, Sinha SN, Shepherd JJ, Shulkes A | title = Peptide alpha-amidation activity in human plasma: relationship to gastrin processing. | journal = Clin. Endocrinol. | volume = 39 | issue = 1 | pages = 51–8 | year = 1993 | pmid = 8102327 | doi = 10.1111/j.1365-2265.1993.tb01750.x }}
*{{cite journal | author=Mains RE, Milgram SL, Keutmann HT, Eipper BA |title=The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins. |journal=Mol. Endocrinol. |volume=9 |issue= 1 |pages= 3-13 |year= 1995 |pmid= 7760848 |doi= }}
* {{cite journal | vauthors = Yun HY, Keutmann HT, Eipper BA | title = Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. | journal = J. Biol. Chem. | volume = 269 | issue = 14 | pages = 10946–55 | year = 1994 | pmid = 8144680 | doi =  }}
*{{cite journal | author=Tateishi K, Arakawa F, Misumi Y, ''et al.'' |title=Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 282-90 |year= 1995 |pmid= 7999037 |doi= 10.1006/bbrc.1994.2662 }}
* {{cite journal | vauthors = Ouafik LH, Mattei MG, Giraud P, Oliver C, Eipper BA, Mains RE | title = Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21. | journal = Genomics | volume = 18 | issue = 2 | pages = 319–21 | year = 1994 | pmid = 8288234 | doi = 10.1006/geno.1993.1471 }}
*{{cite journal | author=Martínez A, Montuenga LM, Springall DR, ''et al.'' |title=Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas. |journal=J. Histochem. Cytochem. |volume=41 |issue= 3 |pages= 375-80 |year= 1993 |pmid= 8094086 |doi= }}
* {{cite journal | vauthors = Husten EJ, Tausk FA, Keutmann HT, Eipper BA | title = Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase. | journal = J. Biol. Chem. | volume = 268 | issue = 13 | pages = 9709–17 | year = 1993 | pmid = 8486658 | doi =  }}
*{{cite journal | author=Kapuscinski M, Green M, Sinha SN, ''et al.'' |title=Peptide alpha-amidation activity in human plasma: relationship to gastrin processing. |journal=Clin. Endocrinol. (Oxf) |volume=39 |issue= 1 |pages= 51-8 |year= 1993 |pmid= 8102327 |doi= }}
* {{cite journal | vauthors = Yun HY, Milgram SL, Keutmann HT, Eipper BA | title = Phosphorylation of the cytosolic domain of peptidylglycine alpha-amidating monooxygenase. | journal = J. Biol. Chem. | volume = 270 | issue = 50 | pages = 30075–83 | year = 1996 | pmid = 8530412 | doi = 10.1074/jbc.270.50.30075 }}
*{{cite journal | author=Yun HY, Keutmann HT, Eipper BA |title=Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. |journal=J. Biol. Chem. |volume=269 |issue= 14 |pages= 10946-55 |year= 1994 |pmid= 8144680 |doi=  }}
* {{cite journal | vauthors = Morris KM, Cao F, Onagi H, Altamore TM, Gamble AB, Easton CJ | title = Prohormone-substrate peptide sequence recognition by peptidylglycine α-amidating monooxygenase and its reflection in increased glycolate inhibitor potency | journal = Bioorganic & Medicinal Chemistry Letters | volume = 22 | issue = 23 | pages = 7015–7018 | date = 1 December 2012 | pmid = 23084901 | doi = 10.1016/j.bmcl.2012.10.004 }}
*{{cite journal | author=Ouafik LH, Mattei MG, Giraud P, ''et al.'' |title=Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21. |journal=Genomics |volume=18 |issue= 2 |pages= 319-21 |year= 1994 |pmid= 8288234 |doi= }}
*{{cite journal | author=Husten EJ, Tausk FA, Keutmann HT, Eipper BA |title=Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9709-17 |year= 1993 |pmid= 8486658 |doi=  }}
*{{cite journal | author=Yun HY, Milgram SL, Keutmann HT, Eipper BA |title=Phosphorylation of the cytosolic domain of peptidylglycine alpha-amidating monooxygenase. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 30075-83 |year= 1996 |pmid= 8530412 |doi= }}
}}
{{refend}}
{{refend}}


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Revision as of 01:50, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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n/a

UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

Peptidyl-glycine alpha-amidating monooxygenase is an enzyme that is required for the biosynthesis of many signaling peptides. This transformation is achieved by conversion of a prohormone to the corresponding amide (C(O)NH2). This enzyme is the only known pathway for generating peptide amides, which renders the peptide more hydrophilic.[1] In humans, PAM is encoded by the PAM gene.[2][3]

Function

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.[3]

The PHM subunit effects hydroxylation of an O-terminal glycine residue:

peptide-C(O)NHCH2CO2− + O2 + 2 [H] → peptide-C(O)NHCH(OH)CO2− + H2O

Involving hydroxylation of a hydrocarbon by O2, this process relies on a copper cofactor. Dopamine beta-hydroxylase, also a copper-containing enzyme, effects a similar transformation.

The PAL subunit then completes the conversion, by catalyzing elimination from the hydroxylated glycine:

peptide-C(O)NHCH(OH)CO2− → peptide-C(O)NH2 + CH(O)CO2−

The eliminated coproduct is glyoxylate, written above as CH(O)CO2−.

References

  1. ↑ Eipper BA, Milgram SL, Husten EJ, Yun HY, Mains RE (1993). "Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains". Protein Sci. 2 (4): 489–97. doi:10.1002/pro.5560020401. PMC 2142366. PMID 8518727.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase".

Further reading

  • Pittner RA, Albrandt K, Beaumont K, Gaeta LS, Koda JE, Moore CX, Rittenhouse J, Rink TJ (1994). "Molecular physiology of amylin". J. Cell. Biochem. 55 Suppl (S1994A): 19–28. doi:10.1002/jcb.240550004. PMID 7929615.
  • Ouafik LH, Stoffers DA, Campbell TA, Johnson RC, Bloomquist BT, Mains RE, Eipper BA (1992). "The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains". Mol. Endocrinol. 6 (10): 1571–84. doi:10.1210/me.6.10.1571. 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. doi:10.1210/me.6.12.1998. PMID 1491686.
  • Braas KM, Harakall SA, Ouafik L, Eipper BA, May V (1992). "Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study". Endocrinology. 130 (5): 2778–88. doi:10.1210/en.130.5.2778. PMID 1572293.
  • Roberts AN, Leighton B, Todd JA, Cockburn D, Schofield PN, Sutton R, Holt S, Boyd Y, Day AJ, Foot EA (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. doi:10.1073/pnas.86.24.9662. PMC 298561. 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. doi:10.1016/0378-1119(95)00364-C. PMID 7590286.
  • Tsukamoto T, Noguchi M, Kayama H, Watanabe T, Asoh T, Yamamoto T (1995). "Increased peptidylglycine alpha-amidating monooxygenase activity in cerebrospinal fluid of patients with multiple sclerosis". Intern. Med. 34 (4): 229–32. doi:10.2169/internalmedicine.34.229. 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. doi:10.1210/me.9.1.3. PMID 7760848.
  • Tateishi K, Arakawa F, Misumi Y, Treston AM, Vos M, Matsuoka Y (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, Treston A, Cuttitta F, Polak JM (1993). "Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas". J. Histochem. Cytochem. 41 (3): 375–80. doi:10.1177/41.3.8094086. PMID 8094086.
  • Kapuscinski M, Green M, Sinha SN, Shepherd JJ, Shulkes A (1993). "Peptide alpha-amidation activity in human plasma: relationship to gastrin processing". Clin. Endocrinol. 39 (1): 51–8. doi:10.1111/j.1365-2265.1993.tb01750.x. 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, Oliver C, Eipper BA, Mains RE (1994). "Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21". Genomics. 18 (2): 319–21. doi:10.1006/geno.1993.1471. PMID 8288234.
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