Literature summary for 2.1.1.6 extracted from

Pedro, A.; Pereira, P.; Bonifacio, M.; Queiroz, J.; Passarinha, L.
Purification of membrane-bound catechol-O-methyltransferase by arginine-affinity chromatography (2015), Chromatographia, 78, 1339-1348.

No PubMed abstract available

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Pichia pastoris	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant membrane-bound isoform, by arginine-affinity chromatography. Optimized conditions for isolation and purification consist in loading of 4 mg of total protein onto the column previously equilibrated at 20 °C and recovery of enzyme in a purified fraction using 500 mM NaCl, 10 mM DTT and 0.5% (v/v) Triton X-100 in 10 mM Tris buffer (pH 7) with a total bioactivity recovery of 24% and 4.95fold purification	Homo sapiens

Purification (Comment)

Organism

recombinant membrane-bound isoform, by arginine-affinity chromatography. Optimized conditions for isolation and purification consist in loading of 4 mg of total protein onto the column previously equilibrated at 20 °C and recovery of enzyme in a purified fraction using 500 mM NaCl, 10 mM DTT and 0.5% (v/v) Triton X-100 in 10 mM Tris buffer (pH 7) with a total bioactivity recovery of 24% and 4.95fold purification

Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.092	-	pH 7.0, 37°C	Homo sapiens

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)