Literature summary for 1.14.17.3 extracted from

Kline, C.D.; Blackburn, N.J.
Substrate-induced carbon monoxide reactivity suggests multiple enzyme conformations at the catalytic copper M-center of peptidylglycine monooxygenase (2016), Biochemistry, 55, 6652-6661 .

Search for more literature for 1.14.17.3

Activating Compound

Activating Compound	Comment	Organism	Structure
O2	substrate binding triggers oxygen activation in peptidylglycine monooygenase	Rattus norvegicus

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of wild-type and mutant enzymes	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
H107A	site-directed mutagenesis, altered reaction with CO compared to wild-type	Rattus norvegicus
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	Rattus norvegicus
H108A	site-directed mutagenesis, altered reaction with CO compared to wild-type	Rattus norvegicus
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	Rattus norvegicus
M109I	site-directed mutagenesis, altered reaction with CO compared to wild-type	Rattus norvegicus
M314H	site-directed mutagenesis, altered reaction with CO compared to wild-type	Rattus norvegicus
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	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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	Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
peptidylglycine + ascorbate + O2	Rattus norvegicus	-	peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P14925	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes	Rattus norvegicus

Reaction

Reaction	Comment	Organism	Reaction ID
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O	equilibrium ordered mechanism in which substrate binds prior to oxygen	Rattus norvegicus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
peptidylglycine + ascorbate + O2	-	Rattus norvegicus	peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O	-	?

Synonyms

Synonyms	Comment	Organism
PHM	-	Rattus norvegicus

Cofactor

Cofactor	Comment	Organism	Structure
ascorbate	-	Rattus norvegicus

General Information

General Information	Comment	Organism
additional information	substrate binding triggers oxygen activation in peptidylglycine monooygenase	Rattus norvegicus

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Release 2023.1 (January 2023)