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Literature summary for 1.14.99.15 extracted from

  • Furuya, T.; Arai, Y.; Kino, K.
    Biotechnological production of caffeic acid by bacterial cytochrome P450 CYP199A2 (2012), Appl. Environ. Microbiol., 78, 6087-6094.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant CYP199A2 in Escherichia coli strain BL21(DE3) Rhodopseudomonas palustris

Protein Variants

Protein Variants Comment Organism
F185A site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
F185G site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
F185I site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
F185L site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme, the F185L mutant exhibits 5.5times higher hydroxylation activity for 4-coumaric acid than the wild-type enzyme Rhodopseudomonas palustris
F185S site-directed mutagenesis, the mutant shows reduced activity with 2-naphthoic acid compared to the wild-type enzyme Rhodopseudomonas palustris
F185T site-directed mutagenesis, the mutant shows reduced activity with 2-naphthoic acid compared to the wild-type enzyme Rhodopseudomonas palustris
F185V site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
F185W site-directed mutagenesis, inactive mutant Rhodopseudomonas palustris
F185Y site-directed mutagenesis, inactive mutant Rhodopseudomonas palustris
additional information substrate specficities of wild-type and F185 mutants, overview Rhodopseudomonas palustris

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Rhodopseudomonas palustris Q6N8N2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-naphthoic acid + AH2 + O2 only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation Rhodopseudomonas palustris 5-hydroxy-2-naphthoic acid + A + H2O
-
?
2-naphthoic acid + AH2 + O2 only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation Rhodopseudomonas palustris 7-hydroxy-2-naphthoic acid + A + H2O
-
?
2-naphthoic acid + AH2 + O2 only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation Rhodopseudomonas palustris 8-hydroxy-2-naphthoic acid + A + H2O
-
?
4-coumaric acid + AH2 + O2 the F185L mutant exhibits 5.5times higher hydroxylation activity for 4-coumaric acid than the wild-type enzyme, good substrate of enzyme mutant F185L, low activity with enzyme mutant sF185V, F185I, F185G, and F185A, moderate activity with the wild-type enzyme and mutants F185Y, F185W, F185S, and F185T with 4-coumaric acid Rhodopseudomonas palustris caffeic acid + A + H2O
-
?
cinnamic acid + AH2 + O2 good substrate of enzyme mutant F185L, and F185G, low activity with enzyme mutants F185V, F185I, F185A F185S, and F185T, no activity with the wild-type enzyme and mutants F185Y and F185W with cinnamic acid Rhodopseudomonas palustris ? + A + H2O
-
?
additional information substrate specficities of wild-type and F185 mutants, overview. The enzyme exhibits oxidation activity for aromatic carboxylic acids, including 2-naphthoic acid, 4-ethylbenzoic acid, and indole-and quinolinecarboxylic acids. No activity of the wild-type enzyme with cinnamic acid Rhodopseudomonas palustris ?
-
?

Synonyms

Synonyms Comment Organism
CYP199A2
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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
7.5
-
assay at Rhodopseudomonas palustris

Cofactor

Cofactor Comment Organism Structure
heme Phe at position 185 is situated directly above, and only 6.35 A from, the heme iron Rhodopseudomonas palustris