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Literature summary for 1.14.17.3 extracted from

  • Takahashi, K.; Satani, M.; Harada, S.; Noguchi, M.
    Expression and characterization of frog peptidylglycine alpha-hydroxylating monooxygenase (2003), Protein Expr. Purif., 27, 35-41.
    View publication on PubMed
Search for more literature for 1.14.17.3

Cloned(Commentary)

Cloned (Comment) Organism
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 Xenopus laevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0011
-
 N-trinitrophenyl-D-Tyr-Val-Gly pH 6.0, 37°C, recombinant enzyme Xenopus laevis
0.057
-
 D-Tyr-Val-Gly pH 7.5, 37°C, recombinant enzyme Xenopus laevis
0.61
-
 hippuric acid pH 5.0, 37°C, recombinant enzyme Xenopus laevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 40000, recombinant enzyme, SDS-PAGE Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Xenopus laevis peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide ?
-
 ?

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from CHO cell culture medium by copper-chelating affinity chromatography Xenopus laevis

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Xenopus laevis
0.85
-
 purified recombinant enzyme, substrate N-trinitrophenyl-D-Tyr-Val-Gly Xenopus laevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Tyr-Val-Gly + ascorbate + O2 synthetic substrate Xenopus laevis D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
-
 ?
hippuric acid + ascorbate + O2 synthetic substrate Xenopus laevis ? + dehydroascorbate + H2O
-
 ir
additional information peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide Xenopus laevis ?
-
 ?
additional information peptide alpha-amidation, the N-terminal substrate structure affects the interaction with the active site of the enzyme Xenopus laevis ?
-
 ?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2 synthetic substrate Xenopus laevis N-trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
-
 ?

Subunits

Subunits Comment Organism
? x * 40000, recombinant enzyme, SDS-PAGE Xenopus laevis

Synonyms

Synonyms Comment Organism
peptidylglycine alpha-hydroxylating monooxygenase
-
 Xenopus laevis
PHM
-
 Xenopus laevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Xenopus laevis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
 hippuric acid pH 5.0, 37°C, recombinant enzyme Xenopus laevis
0.13
-
 D-Tyr-Val-Gly pH 7.5, 37°C, recombinant enzyme Xenopus laevis
1.4
-
 N-trinitrophenyl-D-Tyr-Val-Gly pH 6.0, 37°C, recombinant enzyme Xenopus laevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 with substrate hippuric acid Xenopus laevis
6
-
 with substrate N-trinitrophenyl-D-Tyr-Val-Gly Xenopus laevis
7.5
-
 with substrate D-Tyr-Val-Gly Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Xenopus laevis