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Literature summary for 2.1.1.28 extracted from

  • Kaneda, N.; Hikita, K.; Naruse, Y.; Fukuo, T.; Matsubara, K.; Nagatsu, T.
    Identification of the essential cysteinyl residue located in the active site of human phenylethanolamine N-methyltransferase (1998), Biochem. Biophys. Res. Commun., 249, 405-409.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type enzyme and mutant enzymes in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
C131S mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme Homo sapiens
C139S mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme Homo sapiens
C183S mutant enzyme shows markedly reduced enzyme activity with less than 3% of the maximal activity of the wild-type enzyme, and ca. sixfold increased apparent KM-value for both substrates Homo sapiens
C48S mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme Homo sapiens
C60S mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme Homo sapiens
C91S mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-value of mutant enzymes Homo sapiens
0.0184
-
 norepinephrine wild-type enzyme Homo sapiens
0.0194
-
 S-adenosyl-L-methionine wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
norepinephrine + S-adenosyl-L-methionine
-
 Homo sapiens epinephrine + S-adenosyl-L-homocysteine
-
 ?