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Literature summary for 1.14.15.8 extracted from

  • Bleif, S.; Hannemann, F.; Zapp, J.; Hartmann, D.; Jauch, J.; Bernhardt, R.
    A new Bacillus megaterium whole-cell catalyst for the hydroxylation of the pentacyclic triterpene 11-keto-beta-boswellic acid (KBA) based on a recombinant cytochrome P450 system (2012), Appl. Microbiol. Biotechnol., 93, 1135-1146.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of CYP106A2 by protoplast transformation is only successfully in the plasmid-less Bacillus megaterium strain MS941, not in strain ATCC 13368, coexpression of heterologous redox chain of the P450, bovine adrenodoxin reductase, and bovine adrenodoxin Priestia megaterium

Protein Variants

Protein Variants Comment Organism
additional information recombinant reconstitution of the whole cell conversion of 11-keto-beta-boswellic acid in Bacillus megaterium strain MS941 by coexpression of heterologous redox chain of the P450, bovine adrenodoxin reductase, and bovine adrenodoxin, as well as a a NADPH-regenerating system Priestia megaterium

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a cytochrome P450 enzyme Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-
Priestia megaterium ATCC 13368
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
11-oxo-beta-boswellic acid + reduced ferredoxin + O2 a pentacyclic triterpene, 15beta-hydroxylation Priestia megaterium (3alpha,15beta)-3,15-dihydroxy-11-oxours-12-en-24-oic acid + H2O
-
?
11-oxo-beta-boswellic acid + reduced ferredoxin + O2 a pentacyclic triterpene, 15beta-hydroxylation Priestia megaterium ATCC 13368 (3alpha,15beta)-3,15-dihydroxy-11-oxours-12-en-24-oic acid + H2O
-
?
abietic acid + reduced ferredoxin + O2 a pentacyclic triterpene Priestia megaterium ?
-
?
abietic acid + reduced ferredoxin + O2 a pentacyclic triterpene Priestia megaterium ATCC 13368 ?
-
?
additional information CYP106A2 from hydroxylates a variety of 3-oxo-DELTA4 steroids and catalyzes a one-step regioselective allylic hydroxylation of the diterpene abietic acid Priestia megaterium ?
-
?
additional information CYP106A2 from hydroxylates a variety of 3-oxo-DELTA4 steroids and catalyzes a one-step regioselective allylic hydroxylation of the diterpene abietic acid Priestia megaterium ATCC 13368 ?
-
?

Synonyms

Synonyms Comment Organism
CYP106A2
-
Priestia megaterium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
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
cytochrome P450
-
Priestia megaterium
Ferredoxin
-
Priestia megaterium