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Literature summary for 1.14.13.54 extracted from

  • Franceschini, S.; van Beek, H.L.; Pennetta, A.; Martinoli, C.; Fraaije, M.W.; Mattevi, A.
    Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase (2012), J. Biol. Chem., 287, 22626-22634.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) CodonPlus cells Rhodococcus rhodochrous

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 1.8-2.2 M MgSO4, 0.1 M MES/HCl, pH 6.2-6.5 Rhodococcus rhodochrous

Protein Variants

Protein Variants Comment Organism
K295A the mutant is 3times more active than the wild type enzyme Rhodococcus rhodochrous
L500Y the mutant is about 2.5times more active than the wild type enzyme Rhodococcus rhodochrous
P157Q the mutant shows wild type activity Rhodococcus rhodochrous
T345L the mutation turns the enzyme inactive against progesterone without altering the catalytic efficiency for phenylacetone Rhodococcus rhodochrous
V291A the mutant is less active than the wild type enzyme Rhodococcus rhodochrous

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
phenylacetone mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
0.2
-
phenylacetone mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
0.6
-
phenylacetone mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
0.8
-
phenylacetone mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1
-
phenylacetone wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
2.6
-
phenylacetone mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
progesterone + NADPH + H+ + O2 Rhodococcus rhodochrous
-
Testosterone acetate + NADP+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous O50641
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-affinity column chromatography and Superdex 75 gel filtration Rhodococcus rhodochrous

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenylacetone + NADPH + H+ + O2
-
Rhodococcus rhodochrous benzylacetate + NADP+ + H2O
-
?
progesterone + NADPH + H+ + O2
-
Rhodococcus rhodochrous Testosterone acetate + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
Baeyer-Villiger monooxygenase
-
Rhodococcus rhodochrous
Steroid monooxygenase
-
Rhodococcus rhodochrous
STMO
-
Rhodococcus rhodochrous

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.2
-
phenylacetone mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
0.6
-
phenylacetone mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1
-
phenylacetone mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.5
-
phenylacetone wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.8
-
phenylacetone mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
3
-
phenylacetone mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous

Cofactor

Cofactor Comment Organism Structure
FAD
-
Rhodococcus rhodochrous
NADPH
-
Rhodococcus rhodochrous

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.1
-
progesterone kcat_Km less than 0.1 1/sec*min, mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.2
-
phenylacetone mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.2
-
phenylacetone mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.4
-
progesterone mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.5
-
phenylacetone wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.7
-
progesterone mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
1.8
-
progesterone wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
2.1
-
phenylacetone mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
2.2
-
phenylacetone mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
2.6
-
phenylacetone mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
3.9
-
progesterone mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous
5.2
-
progesterone mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication Rhodococcus rhodochrous