Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant CYP199A2 in Escherichia coli strain BL21(DE3) | Rhodopseudomonas palustris |
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 | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | heme iron | Rhodopseudomonas palustris |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodopseudomonas palustris | Q6N8N2 | - |
- |
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 | Comment | Organism |
---|---|---|
CYP199A2 | - |
Rhodopseudomonas palustris |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Rhodopseudomonas palustris |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Rhodopseudomonas palustris |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | Phe at position 185 is situated directly above, and only 6.35 A from, the heme iron | Rhodopseudomonas palustris |