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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

Reaction

[peptide]-glycine
+ 2 ascorbate +
O2
=
[peptide]-(2S)-2-hydroxyglycine
 + 2 monodehydroascorbate +
H2O

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 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.17.3 peptidylglycine monooxygenase

Cloned

Cloned on EC 1.14.17.3 - peptidylglycine monooxygenase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis
expressed in CHO cells
expressed in CHO DG44 cells
-
expressed in Drosophila S2 cells
expressed in Sf9 cell
-
expression in CHO cells
-
expression in CHO DG44 cells
-
expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-II, wild-type and truncated mutant, N-terminal amino acid sequence analysis
-
expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-III
-
expression in Spodoptera fugiperda cells via baculovirus vector of soluble form 1, AE-I showing only peptidylglycine alpha-hydroxylating activity
-
expression in Spodoptera fugiperda cells via baculovirus vector, amino acid sequence analysis
-
expression of the truncated enzyme, comprising the catalytic core residues 42-356, in CHO DG44 cells
-
gene PAM, DNA and amino acid sequence determination and analysis, genotyping
gene PAM, splice variant PAM-1, recombinant expression of GST-tagged wild-type and mutant PAM-1/H3A enzymes in stable AtT-20 and HEK293 cells cell lines, and recombinant expression of GST-tagged wild-type and mutant PAM-1/H3A enzymes Escherichia coli strain BL21
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
gene PAM-1, recombinant stable expression in murine AtT-20 cells. Atp7a, AP-1, and PAM co-localize in the Golgi region of recombinant AtT-20 cells
medullary thyroid alpha-AE, type A, expression in chinese hamster ovary cells
medullary thyroid carcinoma enzyme, expression in mouse C 127 cells via bovine papilloma virus vector, amino acid and DNA sequence analysis
-
myoblast enzyme, expression in H9c2 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
recombinant expression of wild-type and mutant enzymes
recombinant expression of wild-type and mutant enzymes in CHO DG44 cells
single copy gene, alternative splicing generates several forms of enzyme mRNA, overview
-
stable and functional expression in CHO cells, method establishment, induction of enzyme expression by addition of sodium propionate, N,N'-hexamethylene-bis-acetamide, or best by sodium butyrate, recombinant enzyme is mostly excreted to the medium
-
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
transient expression of wild-type and mutant enzymes in HEK293 cells, stable expression of wild-type and mutant enzymes in CHO cells
-
truncated type A enzyme, expression in mouse C127 cells
-
truncated version (residues 42-356) expressed in CHO cell
-