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Literature summary for 1.14.15.8 extracted from

  • Schumacher, S.D.; Hannemann, F.; Teese, M.G.; Bernhardt, R.; Jose, J.
    Autodisplay of functional CYP106A2 in Escherichia coli (2012), J. Biotechnol., 161, 104-112.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
functional expression of CYP106A2 in Escherichia coli strain BL21 from plasmid pET-CYP13 on the outer membrane with exposure on the surface without the external addition of the heme group but absolutely requiring the coexpression of TolC channel protein JW5503, because Escherichia coli uses a TolC-dependent mechanism to export heme into the growth media, where it can be scavenged by a surface-displayed apoenzyme Priestia megaterium

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a adrenodoxin, heme, and cytochrome P450 containing enzyme Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
11-deoxycorticosterone + reduced adrenodoxin + O2
-
Priestia megaterium 15beta-hydroxy-11-deoxycorticosterone + oxidized adrenodoxin + H2O
-
?
abietic acid + reduced adrenodoxin + O2
-
Priestia megaterium 12-hydroxyabietic acid + oxidized adrenodoxin + H2O
-
?
imipramine + reduced adrenodoxin + O2
-
Priestia megaterium desipramine + oxidized adrenodoxin + H2O
-
?
additional information enzyme reaction is coupled to NADPH oxidation, overview Priestia megaterium ?
-
?

Synonyms

Synonyms Comment Organism
CYP106A2
-
Priestia megaterium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
adrenodoxin dependent on Priestia megaterium
cytochrome P450
-
Priestia megaterium
heme
-
Priestia megaterium