Literature summary for 1.14.15.3 extracted from

Lee, C.; Yu, S.; Lee, J.; Park, S.; Park, H.; Oh, T.; Lee, J.
Crystal structure of a putative cytochrome P450 alkane hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and its conformational substrate binding (2016), Int. J. Mol. Sci., 17, e2067 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 3.1 A resolution, the alkane-like substrate is in the hydrophobic pocket containing residues Thr74, Met90, Ala175, Ile240, Leu241, Val244, Leu292, Met295, and Phe393. Conformational changes in the beta1-beta2, alpha3-alpha4 and alpha6-alpha7 connecting loop are important for incorporating the long hydrophobic substrate	Sphingomonas sp. PAMC 26605

Organism

Organism	UniProt	Comment	Textmining
Sphingomonas sp. PAMC 26605	A0A1S4NYE0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	dodecane strongly binds to Cyp153D17 with similar Kd values as C10-C12 fatty acids	Sphingomonas sp. PAMC 26605	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 48000. SDS-PAGE	Sphingomonas sp. PAMC 26605

Synonyms

Synonyms	Comment	Organism
CYP153D17	-	Sphingomonas sp. PAMC 26605

Cofactor

Cofactor	Comment	Organism	Structure
heme	dodecane, capric acid, and lauric acid binding to CYP153D17 induces a 90% shift in the heme spin state from low-spin (Soret maximum at 420 nm) to high-spin (Soret maximum at 390 nm), whereas decane and myristic acid induces a 80% shift in the same heme spin state	Sphingomonas sp. PAMC 26605

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Release 2023.1 (January 2023)