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Literature summary for 1.14.17.3 extracted from

  • Handa, S.; Spradling, T.J.; Dempsey, D.R.; Merkler, D.J.
    Production of the catalytic core of human peptidylglycine alpha-hydroxylating monooxygenase (hPHMcc) in Escherichia coli (2012), Protein Expr. Purif., 84, 9-13.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.17.3

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0077
-
 N-dansyl-Tyr-Val-Gly pH 6.5, 37°C Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peptidylglycine + ascorbate + O2 Homo sapiens most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P19021
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-

Purification (Commentary)

Purification (Comment) Organism
thioredoxin-hPHMcc-His6 fusion is purified to homogeneity Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-dansyl-Tyr-Val-Gly + ascorbate + O2
-
 Homo sapiens N-dansyl-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
peptidylglycine + ascorbate + O2 most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide Homo sapiens peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?

Subunits

Subunits Comment Organism
More the specific components of the thioredoxin-hPHMcc-His6 fusion protein are as follows: 11.8 kDa for thioredoxin, 5.9 kDa peptide between thioredoxin and hPHMcc, 35.2 kDa for hPMHcc, a 1.5 kDa peptide on the C-terminal side of hPHMcc, and 0.6 kDa for the His6 tag. The sum of the individual masses are 55 kDa, in agreement with the 52 kDa measure by SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
hPHMcc
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 Homo sapiens
peptidylglycine alpha-hydroxylating monooxygenase
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 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.35
-
 N-dansyl-Tyr-Val-Gly pH 6.5, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
physiological function most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
46.8
-
 N-dansyl-Tyr-Val-Gly pH 6.5, 37°C Homo sapiens