1.14.99.15: 4-methoxybenzoate monooxygenase (O-demethylating)
This is an abbreviated version!
For detailed information about 4-methoxybenzoate monooxygenase (O-demethylating), go to the full flat file.
Word Map on EC 1.14.99.15
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1.14.99.15
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putida
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rhodopseudomonas
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palustris
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heme
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benzoic
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ferredoxins
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para-substituted
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regioselectivity
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o-demethylation
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2-naphthoic
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benzene
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putidaredoxin
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dioxygen
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4-hydroxybenzoate
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substrate-free
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couplers
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synthesis
- 1.14.99.15
- putida
- rhodopseudomonas
- palustris
- heme
-
benzoic
- ferredoxins
-
para-substituted
-
regioselectivity
-
o-demethylation
-
2-naphthoic
- benzene
- putidaredoxin
- dioxygen
- 4-hydroxybenzoate
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substrate-free
-
couplers
- synthesis
Reaction
Synonyms
4-methoxybenzoate 4-monooxygenase (O-demethylating), 4-methoxybenzoate monooxygenase, 4-methoxybenzoate O-demethylase, CYP199A2, CYP199A4, cytochrome P450 199A2, oxygenase, 4-methoxybenzoate 4-mono- (O-demethylating), p-anisic O-demethylase, piperonylate-4-O-demethylase, RPA1871
ECTree
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Cofactor
Cofactor on EC 1.14.99.15 - 4-methoxybenzoate monooxygenase (O-demethylating)
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heme
Phe at position 185 is situated directly above, and only 6.35 A from, the heme iron
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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
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palustrisredoxin
i.e. Pux, RPA1872, with [2Fe-2S] cluster
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PuxB, 2Fe-2S ferredoxin, palustrisredoxin B, supports substrate oxidation by CYP199A2
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additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
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additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
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additional information
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the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
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