Literature summary for 1.14.17.3 extracted from

Satani, M.; Takahashi, K.; Sakamoto, H.; Harada, S.; Kaida, Y.; Noguchi, M.
Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase (2003), Protein Expr. Purif., 28, 293-302.

Search for more literature for 1.14.17.3

Cloned(Commentary)

Cloned (Comment)	Organism
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	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	3.26 mol per mol of bifunctional enzyme	Homo sapiens
Cu2+	required for peptidylglycine alpha-hydroxylating monooxygenase activity, 1.25 mol per mol of bifunctional enzyme	Homo sapiens
Fe2+	0.37 mol per mol of bifunctional enzyme	Homo sapiens
Mg2+	0.88 mol per mol of bifunctional enzyme	Homo sapiens
Zn2+	required for peptidylamidoglycolate lyase activity, 0.62 mol per mol of bifunctional enzyme	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
91000	-	x * 91000, recombinant soluble enzyme, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P19021	bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	enzyme contains 2 putative N-glycosylation sites at ASn411 and Asn762, the purified enzyme contains at least 1 sugar chain	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant soluble enzyme from culture medium in a 3-step chromatographic procedure, about 40fold to near homogeneity	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O	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	Homo sapiens	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Homo sapiens	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.53	-	purified recombinant enzyme, peptidylglycine alpha-hydroxylating monooxygenase activity	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-iodo-Tyr-Val-Gly + ascorbate + O2	labeled substrate	Homo sapiens	D-iodo-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O	the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide	?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2	-	Homo sapiens	N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O	the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide	?
peptidylglycine + ascorbate + O2	peptidylglycine alpha-hydroxylating monooxygenase reaction	Homo sapiens	peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O	the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide	?

Subunits

Subunits	Comment	Organism
?	x * 91000, recombinant soluble enzyme, SDS-PAGE	Homo sapiens
More	the enzyme possesses 2 catalytic domains	Homo sapiens

Synonyms

Synonyms	Comment	Organism
bifunctional PAM	-	Homo sapiens
bifunctional peptidylglycine alpha-amidating monooxygenase	-	Homo sapiens
PHM	-	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	7	assay at, dependent on the substrate used	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ascorbate	-	Homo sapiens

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Release 2023.1 (January 2023)