Literature summary for 1.14.14.32 extracted from

Mak, P.J.; Gregory, M.C.; Sligar, S.G.; Kincaid, J.R.
Resonance Raman spectroscopy reveals that substrate structure selectively impacts the heme-bound diatomic ligands of CYP17 (2014), Biochemistry, 53, 90-100.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P05093	cf. EC 1.14.14.19	-

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Release 2023.1 (January 2023)