Literature summary for 1.14.15.35 extracted from

Sen, K.; Thiel, W.
Role of two alternate water networks in compound I formation in P450eryF (2014), J. Phys. Chem. B, 118, 2810-2820.

Search for more literature for 1.14.15.35

Cloned(Commentary)

Cloned (Comment)	Organism
-	Saccharopolyspora erythraea

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics and hybrid quantum mechanics/molecular mechanics analysis. Two water networks exist around the active site, the one found in the crystal structure involving E360 and an alternative one involving E244. The first proton transfer that converts the peroxo to the hydroperoxo intermediate proceeds via the E244 water network with direct involvement of the 5-OH group of the substrate. For the second proton transfer, the computed barriers for the rate-limiting homolytic O-O cleavage are similar for the E360 and E244 pathways, and hence both glutamate residues may serve as proton source in this step	Saccharopolyspora erythraea

Crystallization (Comment)

Organism

molecular dynamics and hybrid quantum mechanics/molecular mechanics analysis. Two water networks exist around the active site, the one found in the crystal structure involving E360 and an alternative one involving E244. The first proton transfer that converts the peroxo to the hydroperoxo intermediate proceeds via the E244 water network with direct involvement of the 5-OH group of the substrate. For the second proton transfer, the computed barriers for the rate-limiting homolytic O-O cleavage are similar for the E360 and E244 pathways, and hence both glutamate residues may serve as proton source in this step

Saccharopolyspora erythraea

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	Q00441	-	-
Saccharopolyspora erythraea NRRL 2338	Q00441	-	-

Synonyms

Synonyms	Comment	Organism
CYP107A1	-	Saccharopolyspora erythraea

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Release 2023.1 (January 2023)