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Information on EC 1.14.17.3 - peptidylglycine monooxygenase and Organism(s) Homo sapiens and UniProt Accession P19021

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IUBMB Comments
A copper protein. 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. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P19021
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-AE, bifunctional PAM, bifunctional peptidylglycine alpha-amidating monooxygenase, CG3832, hPHMcc, More, PAM, PAM-1, PAM-2, PAM-A, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional PAM
277052
-
bifunctional peptidylglycine alpha-amidating monooxygenase
277052
-
hPHMcc
277052
-
PAM-1
277052
-
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
-
-
-
-
peptidylglycine alpha-hydroxylating monooxygenase
peptidylglycine alpha-hydroxylating-monooxygenase
247
-
peptidylglycine alpha-monooxygenase
247
-
peptidylglycine monooxygenase
247
-
peptidylglycine-alpha-amidating monooxygenase
277052
-
synthase, peptide alpha-amide
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxylation
-
-
oxidation
redox reaction
-
-
-
-
reduction
SYSTEMATIC NAME
IUBMB Comments
peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
A copper protein. 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. 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
-
-
-
-
?
D-iodo-Tyr-Val-Gly + ascorbate + O2
D-iodo-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
labeled substrate
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
hippuric acid + ascorbate + O2
glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
insulin + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
insulin glargine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-dansyl-Tyr-Val-Gly + ascorbate + O2
N-dansyl-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
acetyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
alanyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycylvalyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycylvalyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
dansyl-YVG + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-(4-amino-6-methyl-3-oxoheptanoyl)glycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-(phenylacetyl)glycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-decanoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
activity assay
-
-
?
additional information
?
-
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
insulin + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
a POMC 18-kDa fragment
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
3.26 mol per mol of bifunctional enzyme
Fe2+
0.37 mol per mol of bifunctional enzyme
Mg2+
0.88 mol per mol of bifunctional enzyme
Zn2+
required for peptidylamidoglycolate lyase activity, 0.62 mol per mol of bifunctional enzyme
copper
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-(4-dimethylamino)cinnamic acid
-
-
-
(E)-3,4-methylenedioxycinnamic acid
-
-
-
(E)-4-aminocinnamic acid
-
-
-
2-trifluorocinnamic acid
-
-
-
3-(3-pyridyl)acrylic acid
-
-
-
Cinnamic acid
-
extensive dialysis of bifunctional PAM incubated with cinnamate yielded inactive enzyme unable to catalyze the production of glyoxylate from hippuric acid
N-dansyl-4-aminocinnamate
-
a fluorescent molecule, an inactivator
-
perdeuterated cinnamic acid
-
-
-
phenylpropynoic acid
-
i.e. phenylpropiolic acid
-
trans-cinnamic acid
-
-
Urocanic acid
-
-
(acetyloxy)acetic acid
-
-
(decanoylsulfanyl)acetic acid
-
-
(dodecanoyloxy)acetic acid
-
-
([(2S)-2-[(2-aminopropanoyl)amino]-3-phenylpropanoyl]oxy)acetic acid
-
-
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanyl]oxy)acetic acid
-
-
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycyl]oxy)acetic acid
-
-
([[(2S)-1-(2-aminopropanoyl)pyrrolidin-2-yl]carbonyl]oxy)acetic acid
-
-
([[(2S)-1-[[(2-aminopropanoyl)amino]acetyl]pyrrolidin-2-yl]carbonyl]oxy)acetic acid
-
-
([[(4-amino-6-methyl-3-oxoheptanoyl)amino]acetyl]oxy)acetic acid
-
-
4-Phenyl-3-butenoic acid
-
irreversible turnover-dependent inhibition of the enzyme in vitro, at 0.1 mg/ml inhibition in vivo of proliferation of lung cancer cells and Ras-transformed WB rat liver epithelial cells, inhibitor leads to increased gap junction communication in the WB-Ras cells, overview
4-phenyl-3-butenoic acid methyl ester
-
at 0.01 mg/ml inhibition in vivo of proliferation of Ras-transformed WB rat liver epithelial cells, inhibitor leads to increased gap junction communication in the WB-Ras cells, overview
4-phenylbut-3-enoic acid
-
PBA
decanoyloxyacetic acid
-
-
diethyldithiocarbamate
-
DDC
Disulfiram
-
-
S-(2-phenylthioacetyl)thioglycolic acid
-
-
[(phenylacetyl)oxy]acetic acid
-
-
[(phenylacetyl)sulfanyl]acetic acid
-
-
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]oxy]acetic acid
-
-
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]sulfanyl]acetic acid
-
-
[[(2S)-2-([[(2-aminopropanoyl)amino]acetyl]amino)-3-phenylpropanoyl]oxy]acetic acid
-
-
[[(2S)-2-amino-3-phenylpropanoyl]oxy]acetic acid
-
-
[[(2S)-pyrrolidin-2-ylcarbonyl]oxy]acetic acid
-
-
[[(acetylamino)acetyl]oxy]acetic acid
-
-
[[N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanyl]oxy]acetic acid
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0077
N-dansyl-Tyr-Val-Gly
-
pH 6.5, 37C
0.2
alanyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
4
alanyl-L-prolylglycine
-
pH and temperature not specified in the publication
0.035
alanylglycyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
3
alanylglycyl-L-prolylglycine
-
pH and temperature not specified in the publication
0.018
alanylglycylvalyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.96
alanylglycylvalyl-L-prolylglycine
-
pH and temperature not specified in the publication
0.0033 - 0.0194
dansyl-L-Tyr-L-Val-Gly
6.5
L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.88
L-prolylglycine
-
pH and temperature not specified in the publication
0.011
N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.86
N-(4-amino-6-methyl-3-oxoheptanoyl)glycylglycine
-
pH and temperature not specified in the publication
0.33
N-(Phenylacetyl)glycine
-
pH and temperature not specified in the publication
0.015 - 0.016
N-acetyl-L-phenylalanylglycine
9.9
N-acetylglycine
-
pH and temperature not specified in the publication
1.2
N-acetylglycylglycine
-
pH and temperature not specified in the publication
0.2
N-decanoylglycine
-
pH and temperature not specified in the publication
0.007
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.55
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycylglycine
-
pH and temperature not specified in the publication
0.0044 - 0.0068
Trinitrophenyl-D-Tyr-Val-Gly
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
N-dansyl-Tyr-Val-Gly
-
pH 6.5, 37C
0.08 - 13.8
dansyl-L-Tyr-L-Val-Gly
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
46.8
N-dansyl-Tyr-Val-Gly
-
pH 6.5, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 0.0057
4-phenylbut-3-enoic acid
0.00113 - 0.00119
diethyldithiocarbamate
0.00051 - 0.00065
Disulfiram
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
(acetyloxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.007
(decanoylsulfanyl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00006
(dodecanoyloxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.37
([(2S)-2-[(2-aminopropanoyl)amino]-3-phenylpropanoyl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.038
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanyl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.18
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycyl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.29
([[(2S)-1-(2-aminopropanoyl)pyrrolidin-2-yl]carbonyl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
1.1
([[(2S)-1-[[(2-aminopropanoyl)amino]acetyl]pyrrolidin-2-yl]carbonyl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.2
([[(4-amino-6-methyl-3-oxoheptanoyl)amino]acetyl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000096 - 0.00068
4-phenylbut-3-enoic acid
0.00005
decanoyloxyacetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000053 - 0.00011
diethyldithiocarbamate
0.002
[(phenylacetyl)oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.045
[(phenylacetyl)sulfanyl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.006 - 0.011
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]oxy]acetic acid
0.045
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]sulfanyl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.16
[[(2S)-2-([[(2-aminopropanoyl)amino]acetyl]amino)-3-phenylpropanoyl]oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
1.6
[[(2S)-2-amino-3-phenylpropanoyl]oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.5
[[(2S)-pyrrolidin-2-ylcarbonyl]oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
1.8
[[(acetylamino)acetyl]oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.009
[[N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanyl]oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.53
purified recombinant enzyme, peptidylglycine alpha-hydroxylating monooxygenase activity
additional information
-
peptidylglycine alpha-amidating and alpha-hydroxylating monooxygenase activities in several tumor tissue extracts, comparison with immunological analysis, overview, highest activity in medullary thyroid carcinoma
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
assay at, dependent on the substrate used
6
-
assay at
6.5
-
assay at
7.4
-
in vivo assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
integral membrane enzyme
Manually annotated by BRENDA team
-
quantification of PAM endocytic trafficking to the trans-Golgi network
Manually annotated by BRENDA team
-
chromaffin granules
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
AMD_HUMAN
973
1
108332
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
91000
x * 91000, recombinant soluble enzyme, SDS-PAGE
100000
-
PAM, determined by SDS-PAGE and Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 91000, recombinant soluble enzyme, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
enzyme contains 2 putative N-glycosylation sites at ASn411 and Asn762, the purified enzyme contains at least 1 sugar chain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H107A
-
low activity
H108A
-
low activity
M109I
-
low activity
M314H
-
the catalytic activity of the mutant decreases by 96% due to effects on both kcat and KM but it displayed the same activity/pH profile with a maximum around pH 6.0
additional information
-
identification of naurally occuring single nucleotide polymorphisms (SNPs), including the rs13175330 polymorphism. The presence of the G allele of the gene PAM rs13175330 A>G SNP is associated with a higher risk of hypertension after adjustments for age, sex, BMI, smoking, and drinking. The rs13175330 G allele carriers in the hypertension group treated without antihypertensive therapy (HTN w/o therapy) have significantly higher systolic and diastolic blood pressure than the AA genotype carriers, whereas the G allele carriers in the hypertension group treated with antihypertensive therapy (HTN w/ therapy) show significantly higher diastolic blood pressure. The rs13175330 G allele carriers in the HTN w/o therapy group have significantly increased levels of insulin, insulin resistance, and oxidized low-density lipoprotein (LDL) and significantly decreased LDL-cholesterol levels and LDL particle sizes compared to the AA carriers
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells
-
745332
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant PAM from CHO dhfr cells by ammonium sulfate fractionation and anion exchange chromatography
-
recombinant soluble enzyme from culture medium in a 3-step chromatographic procedure, about 40fold to near homogeneity
thioredoxin-hPHMcc-His6 fusion is purified to homogeneity
-
cell extracts are prepared
-
Poros 20 m HQ anion exchange resin column chromatography
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene PAM, DNA and amino acid sequence determination and analysis, genotyping
-
gene PAM, stable recombinant expression of PAM in CHO dhfr cells, construction of pCG/dhfr plasmid with added PAMLID gene incorporating the altered leader sequence
-
gene PAM-1, recombinant stable expression in murine AtT-20 cells
-
production of the catalytic core of human peptidylglycine alpha-hydroxylating monooxygenase (hPHMcc) in Escherichia coli possessing a N-terminal fusion to thioredoxin. Thioredoxin is fused to hPHMcc to enhance the yield of the resulting 52 kDa protein as a soluble and catalytically active enzyme
-
subcloning from human heart lambda-gt10 library in Escherichia coli, soluble recombinant enzyme through elimination of the C-terminal membrane-spanning domain, expression of a soluble form in CHO K-1 cells, excretion of the recombinant enzyme to the cell culture medium
expressed in CHO cells
-
expressed in CHO DG44 cells
-
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
synthesis
-
usage of the recombinant PAM for insulin analogue amidation producing insulin glargine amide, an insulin derivative that shows a time/effect profile which is distinctly more flat and thus more advantageous than insulin glargine itself. The enzyme is used to modify glycine-extended A22(G)-B31(K)-B32(R) human insulin analogue (GKR). Hypoglycemic activity of amidated and non-amidated insulin is compared
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scopsi, L.; Lee, R.; Gullo, M.; Collini, P.; Husten, E.J.; Eipper, B.A.
Peptidylglycine alpha-amidating monooxygenase in neuroendocrine tumors: its identification, characterization, quantification, and relation to the grade of morphologic differentiation, amidated peptide content, and granin immunocytochemistry
Appl. Immunohistochem.
6
120-132
1998
Homo sapiens
-
Manually annotated by BRENDA team
Satani, M.; Takahashi, K.; Sakamoto, H.; Harada, S.; Kaida, Y.; Noguchi, M.
Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase
Protein Expr. Purif.
28
293-302
2003
Homo sapiens, Homo sapiens (P19021)
Manually annotated by BRENDA team
Sunman, J.A.; Foster, M.S.; Folse, S.L.; May, S.W.; Matesic, D.F.
Reversal of the transformed phenotype and inhibition of peptidylglycine alpha-monooxygenase in Ras-transformed cells by 4-phenyl-3-butenoic acid
Mol. Carcinog.
41
231-246
2004
Homo sapiens
Manually annotated by BRENDA team
Klinman, J.P.
The copper-enzyme family of dopamine b-monooxygenase and peptidylglycine a-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
J. Biol. Chem.
281
3013-3016
2006
Homo sapiens
Manually annotated by BRENDA team
Merkler, D.J.; Asser, A.S.; Baumgart, L.E.; Carballo, N.; Carpenter, S.E.; Chew, G.H.; Cosner, C.C.; Dusi, J.; Galloway, L.C.; Lowe, A.B.; Lowe, E.W.; King, L.; Kendig, R.D.; Kline, P.C.; Malka, R.; Merkler, K.A.; McIntyre, N.R.; Romero, M.; Wilcox, B.J.; Owen, T.C.
Substituted hippurates and hippurate analogs as substrates and inhibitors of peptidylglycine alpha-hydroxylating monooxygenase (PHM)
Bioorg. Med. Chem.
16
10061-10074
2008
Blattella germanica, Homo sapiens, Rattus norvegicus (P14925)
Manually annotated by BRENDA team
Trendel, J.A.; Ellis, N.; Sarver, J.G.; Klis, W.A.; Dhananjeyan, M.; Bykowski, C.A.; Reese, M.D.; Erhardt, P.W.
Catalytically active peptidylglycine alpha-amidating monooxygenase in the media of androgen-independent prostate cancer cell lines
J. Biomol. Screen.
13
804-809
2008
Homo sapiens
Manually annotated by BRENDA team
Handa, S.; Spradling, T.J.; Dempsey, D.R.; Merkler, D.J.
Production of the catalytic core of human peptidylglycine alpha-hydroxylating monooxygenase (hPHMcc) in Escherichia coli
Protein Expr. Purif.
84
9-13
2012
Homo sapiens, Homo sapiens (P19021)
Manually annotated by BRENDA team
Bauman, A.T.; Broers, B.A.; Kline, C.D.; Blackburn, N.J.
A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase
Biochemistry
50
10819-10828
2011
Homo sapiens
Manually annotated by BRENDA team
Kline, C.D.; Mayfield, M.; Blackburn, N.J.
HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch
Biochemistry
52
2586-2596
2013
Homo sapiens
Manually annotated by BRENDA team
Morris, K.M.; Cao, F.; Onagi, H.; Altamore, T.M.; Gamble, A.B.; Easton, C.J.
Prohormone-substrate peptide sequence recognition by peptidylglycine alpha-amidating monooxygenase and its reflection in increased glycolate inhibitor potency
Bioorg. Med. Chem. Lett.
22
7015-7018
2012
Homo sapiens
Manually annotated by BRENDA team
Cao, F.; Gamble, A.; Kim, H.; Onagi, H.; Gresser, M.; Kerr, J.; Easton, C.
Potent and selective inhibitors of human peptidylglycine alpha-amidating monooxygenase
MedChemComm
2
760-763
2011
Homo sapiens
-
Manually annotated by BRENDA team
Yoo, H.J.; Kim, M.; Kim, M.; Chae, J.S.; Lee, S.H.; Lee, J.H.
The peptidylglycine-alpha-amidating monooxygenase (PAM) gene rs13175330 A>G polymorphism is associated with hypertension in a Korean population
Hum. Genomics
11
29
2017
Homo sapiens (P19021)
Manually annotated by BRENDA team
Bonnemaison, M.L.; Baeck, N.; Duffy, M.E.; Ralle, M.; Mains, R.E.; Eipper, B.A.
Adaptor protein-1 complex affects the endocytic trafficking and function of peptidylglycine alpha-amidating monooxygenase, a luminal cuproenzyme
J. Biol. Chem.
290
21264-21279
2015
Homo sapiens (P19021), Rattus norvegicus (P14925)
Manually annotated by BRENDA team
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
McIntyre, N.R.; Lowe, E.W.; Battistini, M.R.; Leahy, J.W.; Merkler, D.J.
Inactivation of peptidylglycine alpha-hydroxylating monooxygenase by cinnamic acid analogs
J. Enzyme Inhib. Med. Chem.
31
551-562
2016
Homo sapiens (P19021), Rattus norvegicus (P14925)
Manually annotated by BRENDA team
Zielinski, M.; Wojtowicz-Krawiec, A.; Mikiewicz, D.; Kesik-Brodacka, M.; Cecuda-Adamczewska, V.; Marciniak-Rusek, A.; Sokolowska, I.; Lukasiewicz, N.; Gurba, L.; Odrowaz-Sypniewski, M.; Baran, P.; Plucienniczak, G.; Plucienniczak, A.; Borowicz, P.; Szewczyk, B.
Expression of recombinant human bifunctional peptidylglycine alpha-amidating monooxygenase in CHO cells and its use for insulin analogue modification
Protein Expr. Purif.
119
102-109
2016
Homo sapiens (P19021)
Manually annotated by BRENDA team
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