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Literature summary extracted from

  • Lisurek, M.; Simgen, B.; Antes, I.; Bernhardt, R.
    Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation (2008), Chembiochem, 16, 1439-1449.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.8 expression in Escherichia coli Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.8 A395L Vmax/Km for progesterone is 2fold lower than wild-type value Priestia megaterium
1.14.15.8 E90V/D185G Vmax/Km for progesterone is 1.3fold higher than wild-type value Priestia megaterium
1.14.15.8 G397P the mutant exhibits 2% of the wild-type activity, Vmax/Km for progesterone is 51.7fold lower than wild-type value Priestia megaterium
1.14.15.8 I86T Vmax/Km for progesterone is 2fold higher than wild-type value Priestia megaterium
1.14.15.8 K27R/I71T/I215T Vmax/Km for progesterone is 2.5fold higher than wild-type value Priestia megaterium
1.14.15.8 Q398S Vmax/Km for progesterone is 5fold lower than wild-type value Priestia megaterium
1.14.15.8 S394I Vmax/Km for progesterone is 7.5fold lower than wild-type value Priestia megaterium
1.14.15.8 T396R mutant does not produce any hydroxylated product up to an adrenodoxin concentration of 0.1 mM Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.15.8 0.0007
-
progesterone pH 7.4, 30°C, mutant K27R/I71T/I215T Priestia megaterium
1.14.15.8 0.0009
-
progesterone pH 7.4, 30°C, mutant I86T Priestia megaterium
1.14.15.8 0.001
-
progesterone pH 7.4, 30°C, mutant E90V/D185G Priestia megaterium
1.14.15.8 0.0012
-
deoxycorticosterone pH 7.4, 30°C, mutant I86T Priestia megaterium
1.14.15.8 0.0015
-
progesterone pH 7.4, 30°C, wild-type enzyme Priestia megaterium
1.14.15.8 0.0015
-
deoxycorticosterone pH 7.4, 30°C, wild-type enzyme Priestia megaterium
1.14.15.8 0.0019
-
deoxycorticosterone pH 7.4, 30°C, mutant E90V/D185G Priestia megaterium
1.14.15.8 0.0024
-
progesterone pH 7.4, 30°C, mutant A395L Priestia megaterium
1.14.15.8 0.0024
-
deoxycorticosterone pH 7.4, 30°C, mutant K27R/I71T/I215T Priestia megaterium
1.14.15.8 0.0042
-
deoxycorticosterone pH 7.4, 30°C, mutant A395L Priestia megaterium
1.14.15.8 0.0043
-
progesterone pH 7.4, 30°C, mutant S394I Priestia megaterium
1.14.15.8 0.0046
-
deoxycorticosterone pH 7.4, 30°C, mutant G397P Priestia megaterium
1.14.15.8 0.0047
-
deoxycorticosterone pH 7.4, 30°C, mutant S394I Priestia megaterium
1.14.15.8 0.0049
-
progesterone pH 7.4, 30°C, mutant Q398S Priestia megaterium
1.14.15.8 0.005
-
progesterone pH 7.4, 30°C, mutant G397P Priestia megaterium
1.14.15.8 0.0056
-
deoxycorticosterone pH 7.4, 30°C, mutant Q398S Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.8 Priestia megaterium Q06069 ATCC 13368
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.8
-
Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.8 11-deoxycorticosterone + reduced adrenodoxin + O2 adrenodoxin is a [2Fe-2S] ferredoxin involved in electron transfer from NADPH+ (via a reductase) to cytochrome P-450 in the adrenal gland, 15beta-hydroxy-deoxycorticosterone is the only product that is observed, both in the case of wild-type CYP106A2 and all the mutants (except T396R) Priestia megaterium 15beta-hydroxy-11-deoxycorticosterone + oxidized adrenodoxin + H2O
-
?
1.14.15.8 progesterone + reduced adrenodoxin + O2 adrenodoxin is a [2Fe-2S] ferredoxin involved in electron transfer from NADPH+ (via a reductase) to cytochrome P-450 in the adrenal gland, 15beta-hydroxy-progesterone is the main product of wild-type enzyme and all mutants. In order to gain insights into the structure and function of CYP106A2, whose crystal structure is unknown, a homology model has been created. The substrate progesterone is then docked into the active site to predict which residues might affect substrate binding. The model is substantiated by using a combination of theoretical and experimental investigations Priestia megaterium 15beta-hydroxy-progesterone + oxidized adrenodoxin + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.8 CYP106A2
-
Priestia megaterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.15.8 30
-
assay at Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.8 7.4
-
assay at Priestia megaterium