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1.14.14.32: 17alpha-hydroxyprogesterone deacetylase

This is an abbreviated version!
For detailed information about 17alpha-hydroxyprogesterone deacetylase, go to the full flat file.

Word Map on EC 1.14.14.32

Reaction

17alpha-hydroxypregnenolone
+
[reduced NADPH-hemoprotein reductase]
+
O2
=
3beta-hydroxyandrost-5-en-17-one
+
acetate
+
[oxidized NADPH-hemoprotein reductase]
+
H2O

Synonyms

17,20 lyase, 17-20 lyase, 17-alpha-hydroxylase/C17-20 lyase, 17-hydroxylase/C17,20-lyase, 17alpha-hydroxylase, 17alpha-hydroxylase-C(17,20)-lyase, 17alpha-hydroxylase-C17,20-lyase, 17alpha-hydroxylase/17,20 lyase, 17alpha-hydroxylase/17,20-lyase, 17alpha-hydroxylase/17,20-lyase cytochrome P450, 17alpha-hydroxylase/C(17,20)-lyase, 17alpha-hydroxylase/C17,20-lyase, 17alpha-hydroxyprogesterone aldolase, 17alpha-hydroxyprogesterone aldolase/17,20-lyase, 17alpha-lyase, Adrenal 17,20-lyase, aldolase, 17alpha-hydroxyprogesterone, C-17,20 lyase, C-17/C-20 lyase, C17(20) lyase, C17,20 lyase, C17,20-lyase, CYP17, CYP17A1, cytochrome P450 17, cytochrome P450 17A1, cytochrome P450 17alpha-hydroxylase/17,20-lyase, cytochrome p450 17alpha-hydroxylase/C(17,20)-lyase, cytochrome P450c17, EC 4.1.2.30, P-45017alpha, P450 17A1, P45017alpha, P450c17, P450c17-I, steroid 17alphahydroxylase/17,20-lyase, Steroid C17(20) lyase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.32 17alpha-hydroxyprogesterone deacetylase

Crystallization

Crystallization on EC 1.14.14.32 - 17alpha-hydroxyprogesterone deacetylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
resonance Raman spectroscopy of ferric form reveals that binding of substrate causes variable degrees of conversion from the low spin to high spin state, with the nonhydroxylated progesterone and pregnenolone yielding almost complete high spin form, while the two hydroxylated substrates (17-hydroxyprogesterone and 17-hydroxypregnenolone) give only about a 60% conversion to high spin. The heme structure and its interactions with the active site protein residues remain constant for all four substrates