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Literature summary extracted from

  • Janocha, S.; Carius, Y.; Hutter, M.; Lancaster, C.R.; Bernhardt, R.
    Crystal structure of CYP106A2 in substrate-free and substrate-bound form (2016), ChemBioChem, 17, 852-860 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.15.8 substrate-free enzyme to 1.8 A resolution, cocrystallization of CYP106A2 with abietic acid reveals bending of the heme cofactor when abietic acid is bound in the active site Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.8 Priestia megaterium Q06069 isoform Cyp106A2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.8 abietic acid + reduced adrenodoxin + O2 binding of abietic acid results in a type II difference spectrum typical for nitrogenous inhibitors Priestia megaterium ? + oxidized adrenodoxin + H2O
-
 ?
1.14.15.8 dehydroabietic acid + reduced adrenodoxin + O2
-
 Priestia megaterium ? + oxidized adrenodoxin + H2O
-
 ?
1.14.15.8 isopimaric acid + reduced adrenodoxin + O2
-
 Priestia megaterium ? + oxidized adrenodoxin + H2O
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.8 heme presence of dehydroabietic acid does not induce a high-spin shift of the enzyme Priestia megaterium