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Literature summary for 1.14.99.15 extracted from

  • Bell, S.G.; Xu, F.; Johnson, E.O.; Forward, I.M.; Bartlam, M.; Rao, Z.; Wong, L.L.
    Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris (2009), J. Biol. Inorg. Chem., 15, 315-328.
    View publication on PubMed
Search for more literature for 1.14.99.15

Cloned(Commentary)

Cloned (Comment) Organism
-
 Rhodopseudomonas palustris

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ [Fe2-S2]-cluster in the cofactors, overview Rhodopseudomonas palustris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-methoxybenzoate + AH2 + O2 Rhodopseudomonas palustris
-
 4-hydroxybenzoate + formaldehyde + A + H2O
-
 ?
4-methoxybenzoate + AH2 + O2 Rhodopseudomonas palustris CGA009
-
 4-hydroxybenzoate + formaldehyde + A + H2O
-
 ?
4-methoxybenzoate + reduced palustrisredoxin + O2 Rhodopseudomonas palustris
-
 4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
 ?
4-methoxybenzoate + reduced palustrisredoxin + O2 Rhodopseudomonas palustris CGA009
-
 4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
 ?
additional information Rhodopseudomonas palustris CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview ?
-
 ?
additional information Rhodopseudomonas palustris CGA009 CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodopseudomonas palustris
-
 CGA009
-
Rhodopseudomonas palustris
-
 gene RPA1871
-
Rhodopseudomonas palustris CGA009
-
 CGA009
-
Rhodopseudomonas palustris CGA009
-
 gene RPA1871
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rhodopseudomonas palustris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methoxybenzoate + AH2 + O2
-
 Rhodopseudomonas palustris 4-hydroxybenzoate + formaldehyde + A + H2O
-
 ?
4-methoxybenzoate + AH2 + O2
-
 Rhodopseudomonas palustris CGA009 4-hydroxybenzoate + formaldehyde + A + H2O
-
 ?
4-methoxybenzoate + reduced palustrisredoxin + O2
-
 Rhodopseudomonas palustris 4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
 ?
4-methoxybenzoate + reduced palustrisredoxin + O2
-
 Rhodopseudomonas palustris CGA009 4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
 ?
additional information CYP199A2 is a heme monooxygenase that catalyses the oxidation of para-substituted benzoic acids, the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation Rhodopseudomonas palustris ?
-
 ?
additional information CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview Rhodopseudomonas palustris ?
-
 ?
additional information CYP199A2 is a heme monooxygenase that catalyses the oxidation of para-substituted benzoic acids, the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation Rhodopseudomonas palustris CGA009 ?
-
 ?
additional information CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview Rhodopseudomonas palustris CGA009 ?
-
 ?

Synonyms

Synonyms Comment Organism
4-methoxybenzoate monooxygenase
-
 Rhodopseudomonas palustris
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
7.4
-
 the electron transfer to CYP199A2 is studied Rhodopseudomonas palustris

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
 Rhodopseudomonas palustris
heme
-
 Rhodopseudomonas palustris
additional information PuxB, 2Fe-2S ferredoxin, palustrisredoxin B, supports substrate oxidation by CYP199A2 Rhodopseudomonas palustris
palustrisredoxin CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview. Interaction of CYP199A2 with PuxB mutants, structure of PuxB A105R, and with ferredoxin, detailed overview. RPA3956, PuxB, from strain CGA009 is a vertebrate-type [2Fe-2S] ferredoxin with the characteristic cysteine in ferredoxins involved in Fe-S cluster biogenesis, PuxB also supports substrate oxidation by CYP199A2 Rhodopseudomonas palustris

General Information

General Information Comment Organism
physiological function CYP199A2 catalyzes the oxidative demethylation of 4-methoxybenzoic acid and the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation by this organism Rhodopseudomonas palustris