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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.14.99.15 F185A site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
1.14.99.15 F185G site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
1.14.99.15 F185I site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
1.14.99.15 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
1.14.99.15 F185S site-directed mutagenesis, the mutant shows reduced activity with 2-naphthoic acid compared to the wild-type enzyme Rhodopseudomonas palustris
1.14.99.15 F185T site-directed mutagenesis, the mutant shows reduced activity with 2-naphthoic acid compared to the wild-type enzyme Rhodopseudomonas palustris
1.14.99.15 F185V site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme Rhodopseudomonas palustris
1.14.99.15 F185W site-directed mutagenesis, inactive mutant Rhodopseudomonas palustris
1.14.99.15 F185Y site-directed mutagenesis, inactive mutant Rhodopseudomonas palustris
1.14.99.15 additional information substrate specficities of wild-type and F185 mutants, overview Rhodopseudomonas palustris

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.15 Rhodopseudomonas palustris Q6N8N2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.15 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
-
 ?
1.14.99.15 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
-
 ?
1.14.99.15 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
-
 ?
1.14.99.15 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
-
 ?
1.14.99.15 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
-
 ?
1.14.99.15 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

EC Number Synonyms Comment Organism
1.14.99.15 CYP199A2
-
 Rhodopseudomonas palustris

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.99.15 30
-
 assay at Rhodopseudomonas palustris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.99.15 7.5
-
 assay at Rhodopseudomonas palustris

Cofactor

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