Literature summary for 1.14.99.15 extracted from

Bell, S.G.; Xu, F.; Forward, I.; Bartlam, M.; Rao, Z.; Wong, L.L.
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris (2008), J. Mol. Biol., 383, 561-574.

Search for more literature for 1.14.99.15

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of the His-tagged enzyme in Escherichia coli BL21(DE3)	Rhodopseudomonas palustris

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant CYP199A2, 16 ºC, the hanging drop vapor diffusion method under aerobic conditions, 0.0015 ml of protein solution is mixed with 0.0015 ml of reservoir solution, addition of 200 ml reservoir solution, containing 15% PEG 4000, 100 mM sodium citrate pH 5.6, 20% isopropanol with 4% v/v t-butanol, 1 week, X-ray diffraction structure deternnation and analysis at 2.0 A resolution	Rhodopseudomonas palustris

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	steady-state kinetics	Rhodopseudomonas palustris

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	heme iron	Rhodopseudomonas palustris

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
4-methoxybenzoate + reduced ferredoxin + O2	Rhodopseudomonas palustris	-	4-hydroxybenzoate + formaldehyde + ferredoxin + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Rhodopseudomonas palustris	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration	Rhodopseudomonas palustris

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-ethylbenzoate + AH2 + O2	a C-C bond dehydrogenation of an unbranched alkyl group, computational docking of 4-ethylbenzoate into the active site suggests that the substrate carboxylate oxygens interact with Ser97 and Ser247, and the beta-methyl group is located over the heme iron by Phe185, this binding orientation is consistent with the observed product profile of exclusive attack at the para substituent, overview	Rhodopseudomonas palustris	4-(1-hydroxyethyl)-benzoate + 4-vinylbenzoate + A + H2O	-	?
4-methoxybenzoate + reduced ferredoxin + O2	-	Rhodopseudomonas palustris	4-hydroxybenzoate + formaldehyde + ferredoxin + H2O	-	?
4-methoxybenzoate + reduced putidaredoxin + O2	very low activity with putidaredoxin	Rhodopseudomonas palustris	4-hydroxybenzoate + formaldehyde + oxidized putidaredoxin + H2O	-	?
additional information	CYP199A2 shows a strong preference for para-substituted benzoate over identically substituted ortho- and meta- benzoates, and para-substituted benzenes, benzyl alcohols and benzaldehydes, a cytochrome P450 enzyme, the substrate binding pocket is hydrophobic, with Ser97 and Ser247 being the only polar residues, substrate binding and substrate channeling mechanism and structure, overview	Rhodopseudomonas palustris	?	-	?

Synonyms

Synonyms	Comment	Organism
CYP199A2	-	Rhodopseudomonas palustris

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Rhodopseudomonas palustris

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Rhodopseudomonas palustris

Cofactor

Cofactor	Comment	Organism	Structure
reduced ferredoxin	-	Rhodopseudomonas palustris

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Release 2023.1 (January 2023)