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
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results (Metals Ions
Metals Ions on EC 1.14.17.3 - peptidylglycine monooxygenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
copper
Cu2+
Zn2+
additional information
Ag(I) is iso-electronic with Cu(I) and has been shown to be handled by similar cellular transport processes. Although complexes of Ag in the Ag(III) state exists, the instability of the Ag(II) state renders the metal unsuitable for a functional substitute for copper in enzymes such as PHM. When enzyme mutants H107A/H108A and M109I (a wild-type analogue with both copper sites intact) are incubated with excess AgNO3, each variant binds a single Ag(I) ion, from which it is inferred that Ag(I) binds selectively at the M-center with little or no affinity for the H-center
copper
essentially required for activity, 2 atoms bound by 5 conserved His residues and 1 conserved Met residue
copper
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dependent on, copper-deficiency decreases the enzyme activity, tissue copper status, overview
copper
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dependent on, copper-deficiency decreases the enzyme activity, tissue copper status, overview
copper
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inter-copper electron transfer, mechanism, structure, 2 copper atoms per enzyme
copper
two distinct Cu centers are located in the protein active site. Of the two distinct Cu centers in the protein active site (separated by 11 A), the CuH site, believed to serve primarily as an electron transfer site, is coordinated by three histidines, H107, H108, H172, in a roughly T-shaped geometry. The CuM site, where oxygen binding and hydroxylation occur, has a mixed coordination sphere consisting of two histidines, H242, and H244, and a methionine, M314. Reaction mechanism, overview. Reaction of wild-type enzyme PHM with CO (an oxygen analogue) produces the M-site CO complex, which shows a unique XES spectrum that can be computationally reproduced by including interactions between Cu(I) and the CO ligand. The valence-to-core (VtC) region can serve as a probe of not only ligand speciation, but also offer insight into the coordination geometry, in a fashion similar to XAS pre-edges, and may be sufficiently sensitive to the coordination of exogenous ligands to be useful in the study of reaction mechanisms. Application of X-ray emission spectroscopy to copper proteins via a study of a series of mixed His-Met copper sites where the ligand set varies in a systematic way between the His3 and Met3 limits. The sites are derived from the wild-type peptidylglycine monooxygenase (PHM), two single-site variants which replicate each of its two copper sites (CuM-site and CuH-site), and the transporters CusF and CusB. Structure analysis of copper centers of wild-type and mutant enzymes
Cu2+
required for peptidylglycine alpha-hydroxylating monooxygenase activity, 1.25 mol per mol of bifunctional enzyme
Cu2+
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The enzyme contains two copper centers, one performs the substrate hydroxylation, while the second is used for electron storage/transfer
Cu2+
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mutant H172A has reduced copper content: below 0.3 Cu2+ per protein molecule
Cu2+
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oxygen activation by the noncoupled binuclear copper site, analysis of structure and electron transfer mechanism, formation of a CuIIM-OOH reaction intermediate, thermodynamics
Cu2+
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required, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species
Cu2+
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a copper enzyme, copper binding ratios of recombinant catalytic core, overview
Cu2+
a bicopper enzyme, two noninteracting copper atoms, involved in reaction mechanism, detailed overview
Cu2+
a dicopper enzyme, copper reconstitution of recombinant purified wild-type and mutant enzymes, modeling of the active site structure of PHM showing the M-center and H-center with substrate, overview
Cu2+
a pair of uncoupled copper centers separated by 11 A termed CuH and CuM, an unusual Cu(I)S-Met interaction at the oxygen binding M-site, and the postulated Cu(II)-superoxo intermediate, structure and chemistry of the individual metal centers. The copper centers are involved in the catalytic mechanism, the M-center binds two histidines and a methionine at all pHs, while the H-center is two-coordinate at neutral pH but coordinated another methionine S ligand at low pH. Analysis of CO complex formations of wild-type and mutant enzymes at pH 3.5-7.5, detailed overview
Cu2+
dependent on, two coopper ions, CuM is coordinated by His242, His244 and Met314, while CuH is bound to His107, His108, and His172. The catalytic reaction requires both copper ions to cycle between Cu(II) and Cu(I) oxidation states. Two conformations at CuM in which the second CO band depends on the mode of substrate binding and may thus report on a substrate-induced catalytically active configuration. Upon substrate addition, the lower (nyCO) band is amplified while the other decreases, but not at a 1:1 ratio, indicating an equilibrium which is shifted in the presence of substrate. Crystal structure of CuM and CuH sites, overview
Cu2+
the cuproenzyme PAM requires copper to catalyze peptide amidation
Zn2+
required for peptidylamidoglycolate lyase activity, 0.62 mol per mol of bifunctional enzyme
