Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.17.3 - peptidylglycine monooxygenase and Organism(s) Drosophila melanogaster and UniProt Accession O01404

for references in articles please use BRENDA:EC1.14.17.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A copper protein. The enzyme binds two copper ions with distinct roles during catalysis. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. In mammals, the two activities are part of a bifunctional protein. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Drosophila melanogaster
UNIPROT: O01404
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
peptidylglycine alpha-hydroxylating monooxygenase, bifunctional pam, peptidylglycine monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, alpha-ae, phmcc, peptidylglycine alpha-amidating mono-oxygenase, pam-b, peptidylglycine alpha-monooxygenase, peptidylglycine-alpha-amidating monooxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptidylglycine alpha-amidating monooxygenase
-
peptidylglycine alpha-hydroxylating monooxygenase
-
PAM
-
-
-
-
PAM-A
-
-
-
-
PAM-B
-
-
-
-
peptide alpha-amidating enzyme
-
-
-
-
peptide alpha-amide synthase
-
-
-
-
peptide-alpha-amide synthetase
-
-
-
-
peptidyl alpha-amidating enzyme
-
-
-
-
peptidylglycine 2-hydroxylase
-
-
-
-
peptidylglycine alpha-amidating monooxygenase
-
-
-
-
peptidylglycine alpha-hydroxylase
-
-
-
-
synthase, peptide alpha-amide
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[peptide]-glycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
A copper protein. The enzyme binds two copper ions with distinct roles during catalysis. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. In mammals, the two activities are part of a bifunctional protein. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
CAS REGISTRY NUMBER
COMMENTARY hide
90597-47-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chromogranin A + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM. PAM-dependent amidation of POMC peptides in AtT20 cells
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM. PAM-dependent amidation of POMC peptides in AtT20 cells
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
neuroendocrine Tv cells of larval brains
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
peptidylglycine alpha-amidating monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important posttranslational modification. Peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, physiological effects of hypoxia may be PAM-dependent. PHM-dependent amidation of POMC peptides is sensitive to oxygen in AtT20 cells. Enzyme PHM is essential for development in Drosophila melanogaster. Peptidylglycine alpha-amidating monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important posttranslational modification. Peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, physiological effects of hypoxia may be PAM-dependent. Because PAM-dependent amidation is irreversible, bi-directional responses that rapidly upregulate and downregulate levels of amidation can only be observed on rapidly turned-over PAM substrates
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHM_DROME
365
1
40564
Swiss-Prot
Secretory Pathway (Reliability: 1)
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells
745332
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
enzyme PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Simpson, P.D.; Eipper, B.A.; Katz, M.J.; Gandara, L.; Wappner, P.; Fischer, R.; Hodson, E.J.; Ratcliffe, P.J.; Masson, N.
Striking oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells
J. Biol. Chem.
290
24891-24901
2015
Drosophila melanogaster (O01404), Homo sapiens (P19021), Mus musculus (P97467)
Manually annotated by BRENDA team