1.14.17.3: peptidylglycine monooxygenase
This is an abbreviated version!
For detailed information about peptidylglycine monooxygenase, go to the full flat file.
Word Map on EC 1.14.17.3
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1.14.17.3
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glycine-extended
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neuropeptides
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beta-monooxygenase
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peptidyl-alpha-hydroxyglycine
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prohormone
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alpha-hydroxyglycine
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peptidylamidoglycolate
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endoproteolytic
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neurointermediate
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corticotrope
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ascorbate-dependent
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exafs
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4.3.2.5
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4-phenyl-3-butenoic
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noncoupled
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side-on
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dbetam
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medicine
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analysis
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synthesis
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pharmacology
- 1.14.17.3
-
glycine-extended
- neuropeptides
-
beta-monooxygenase
-
peptidyl-alpha-hydroxyglycine
-
prohormone
- alpha-hydroxyglycine
- peptidylamidoglycolate
-
endoproteolytic
-
neurointermediate
-
corticotrope
-
ascorbate-dependent
-
exafs
-
4.3.2.5
-
4-phenyl-3-butenoic
-
noncoupled
-
side-on
- dbetam
- medicine
- analysis
- synthesis
- pharmacology
Reaction
Synonyms
alpha-AE, bifunctional PAM, bifunctional peptidylglycine alpha-amidating monooxygenase, CG3832, hPHMcc, More, PAM, PAM-1, PAM-2, PAM-A, PAM-B, PAM/PHM, peptide alpha-amidating enzyme, peptide alpha-amide synthase, peptide-alpha-amide synthetase, peptidyl alpha-amidating enzyme, peptidyl alpha-hydroxylating monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, peptidylglycine 2-hydroxylase, peptidylglycine alpha-amidating mono-oxygenase, peptidylglycine alpha-amidating monooxygenase, peptidylglycine alpha-hydroxylase, peptidylglycine alpha-hydroxylating monooxygenase, peptidylglycine alpha-hydroxylating-monooxygenase, peptidylglycine alpha-monooxygenase, peptidylglycine monooxygenase, peptidylglycine-alpha-amidating monooxygenase, PHM, PHMcc, synthase, peptide alpha-amide, type A PAM
ECTree
1.14.17.3 peptidylglycine monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.17.3 - peptidylglycine monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H172A
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coppper biniding similar to wild type, but showed a 1000fold decrease in turnover rate
M314H
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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
H364A/H366A/H367A
site-directed mutagenesis. mutant PAM-1/H3A shows affected trafficking through the endogenous membranes. The PAM-1/H3A mutant exhibits the same pH optimum as the wild-type of pH 4.5, but shows slightly lower activity from pH 5.5-7.0. Mutant PAM-1/H3A and wild-type PAM-1 are processed differently when expressed in AtT-20 corticotrope tumor cells. Proteolytic processing of PAM-1 and PAM-1/H3A in AtT-20 cells is similar. Newly synthesized PAM-1/H3A disappears more quickly than newly synthesized PAM-1 in the cells. The H3A mutation eliminates the ability of internalized PAM-1 to return to secretory granules. Alkalinizing agents show differential effects on PAM-1 and PAM-1/H3A. Phenotype comparisons of wild-type and mutant enzymes and enzyme expressing cells, overview
H107A
H107A/H108A
H108A
H172A
H242A
M109I
site-directed mutagenesis, altered reaction with CO compared to wild-type
M314H
site-directed mutagenesis, altered reaction with CO compared to wild-type
M314I
site-directed mutagenesis, the CuM site mutant which has an empty M site in the reduced state, does not react with CO in the presence or absence of peptide substrate
Q170A
Q170E
Q170L
Q170N
Y318F
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site-directed mutagenesis, active site residue mutant, slightly reduced rate constant for C-H bond cleavage compared to the wild-type enzyme
Y79W
additional information
H107A
site-directed mutagenesis, altered reaction with CO compared to wild-type
H107A
site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes
H107A/H108A
site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes
H107A/H108A
site-directed mutagenesis, removal of two of three histidines prevents metal binding at the H-center, the double His mutant H107H108A binds copper only in the M-site and therefore contains about 1 equivalent copper per protein. The PHM variant, when metalated, binds copper and silver at only a single center
H107A/H108A
site-directed mutagenesis, structure analysis of copper centers compared to wild-type
H107A/H108A
site-directed mutagenesis, the double His mutant H107H108A binds copper only in the M-site and therefore contains about 1 equivalent copper per protein
H108A
site-directed mutagenesis, altered reaction with CO compared to wild-type
H108A
site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes
H172A
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mutant of copper ligand of peptidylglycine alpha-hydroxylating enzyme, reduced copper content below 0.3 Cu2+ per protein molecule
H172A
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mutation in the copper center of domain one, no activity in presence of H2O2
H172A
site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes
H242A
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mutation in the copper center of domain two, no activity in presence of H2O2
H242A
site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes
H242A
site-directed mutagenesis, structure analysis of copper centers compared to wild-type
H242A
site-directed mutagenesis, the CuM site mutant which has an empty M site in the reduced state, does not react with CO in the presence or absence of peptide substrate
H242A
site-directed mutagenesis, the CuM site mutant which has an empty M site in the reduced state, does not react with CO in the presence or absence of peptide substrate. The PHM variant, when metalated, binds copper and silver at only a single center. The H242A variant is an M-site deletion mutant that removes one of the two histidines necessary for tight binding of copper to the M-site
Q170A
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site-directed, PCR-based mutagenesis, altered Km compared to the wild-type enyme
Q170A
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site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Q170E
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site-directed, PCR-based mutagenesis, kinetics similar to the wild-type enyme
Q170E
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site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Q170L
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site-directed, PCR-based mutagenesis, kinetics similar to the wild-type enyme
Q170L
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site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Q170N
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site-directed, PCR-based mutagenesis, kinetics similar to the wild-type enyme
Q170N
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site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Y79W
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site-directed, PCR-based mutagenesis, altered kinetics compared to the wild-type enzyme, highly reduced activity
Y79W
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site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
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
additional information
siRNA knockdown of PAM is accompanied by a loss of 18 kDa JP-NH2 immunoactivity with gamma3-MSH immunoactivity remaining unaffected
additional information
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only the residues 42-356 carrying the monoogenase domain was expressed
additional information
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only the residues 42-356 carrying the monoogenase domain was expressed
additional information
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large scale production of the enzyme using an automated bioreactor, method optimization and evaluation, overview
additional information
comparison of the first electron transfer step (reductive phase) in the wild-type enzyme PHM as well as its mutant variants. Stopped-flow is used to record the reduction kinetic traces using the chromophoric agent N,N-dimethyl-4-phenylenediamine (DMPD) as the reductant
additional information
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construction of a truncated form of AE-II, lacking the transmembrane domain and leading to solubility of the fully active, truncated enzyme being secreted into the culture medium from Spodoptera frugiperda cells
