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Literature summary for 1.14.17.3 extracted from

  • Chauhan, S.; Hosseinzadeh, P.; Lu, Y.; Blackburn, N.J.
    Stopped-flow studies of the reduction of the copper centers suggest a bifurcated electron transfer pathway in peptidylglycine monooxygenase (2016), Biochemistry, 55, 2008-2021 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.17.3

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in CHO DG44 cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
H107A site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes Rattus norvegicus
H107A/H108A site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes Rattus norvegicus
H108A site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes Rattus norvegicus
H172A site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes Rattus norvegicus
H242A site-directed mutagenesis, comparison of stopped-flow reduction kinetics of wild-type and mutant enzymes Rattus norvegicus
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 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information stopped-flow reduction kinetics of wild-type and mutant enzymes using the chromophoric agent N,N-dimethyl-4-phenylenediamine (DMPD) as the reductant, overview Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
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 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 from CHO DG44 cells. Copper reconstitution of recombinant purified 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 stopped-flow studies of the reduction of the copper centers suggest a bifurcated electron transfer pathway in peptidylglycine monooxygenase Rattus norvegicus
a

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PHM
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Rattus norvegicus