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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, MUTAGENESIS OF GLY-490, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
STRAIN=ACB;
PubMed=11322873 [NCBI, ExPASy, EBI, Israel, Japan]
Kamerbeek N.M.,
Moonen M.J.H.,
van der Ven J.G.M.,
van Berkel W.J.H.,
Fraaije M.W.,
Janssen D.B.;
"4-hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds.";
Eur. J. Biochem. 268:2547-2557(2001).
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[2]
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MUTAGENESIS OF HIS-296 AND TRP-300.
STRAIN=ACB;
DOI=10.1016/S0014-5793(02)02623-6; PubMed=11997015 [NCBI, ExPASy, EBI, Israel, Japan]
Fraaije M.W.,
Kamerbeek N.M.,
van Berkel W.J.H.,
Janssen D.B.;
"Identification of a Baeyer-Villiger monooxygenase sequence motif.";
FEBS Lett. 518:43-47(2002).
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[3]
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FUNCTION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ACB;
DOI=10.1128/AEM.69.1.419-426.2003; PubMed=12514023 [NCBI, ExPASy, EBI, Israel, Japan]
Kamerbeek N.M.,
Olsthoorn A.J.J.,
Fraaije M.W.,
Janssen D.B.;
"Substrate specificity and enantioselectivity of 4-hydroxyacetophenone monooxygenase.";
Appl. Environ. Microbiol. 69:419-426(2003).
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[4]
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MUTAGENESIS OF ARG-339; LYS-439 AND ARG-440, KINETIC PARAMETERS, AND ENZYME REGULATION.
STRAIN=ACB;
DOI=10.1111/j.1432-1033.2004.04126.x; PubMed=15153101 [NCBI, ExPASy, EBI, Israel, Japan]
Kamerbeek N.M.,
Fraaije M.W.,
Janssen D.B.;
"Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases.";
Eur. J. Biochem. 271:2107-2116(2004).
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[5]
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MASS SPECTROMETRY, AND REACTION MECHANISM.
DOI=10.1074/jbc.M503758200; PubMed=16049018 [NCBI, ExPASy, EBI, Israel, Japan]
van den Heuvel R.H.H.,
Tahallah N.,
Kamerbeek N.M.,
Fraaije M.W.,
van Berkel W.J.H.,
Janssen D.B.,
Heck A.J.R.;
"Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase.";
J. Biol. Chem. 280:32115-32121(2005).
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- FUNCTION: Catalyzes a Baeyer-Villiger oxidation reaction, i.e., the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Can oxidize a wide range of acetophenone derivatives. Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring, e.g. 4-hydroxyacetophenone and 4-aminoacetophenone, leading to the formation of 4-hydroxyphenyl acetate and 4-aminophenyl acetate, respectively. Is also able to oxidize sulfides.
- CATALYTIC ACTIVITY: (4-hydroxyphenyl)ethan-1-one + NADPH + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O.
- COFACTOR: Binds 1 FAD per subunit.
- ENZYME REGULATION: Inhibited by amino-NADP(+).
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=12 µM for NADPH (at pH 7.5); | | KM=1.44 mM for NADH (at pH 7.5); | | KM=9.2 µM for 4-hydroxyacetophenone (at pH 7.5); | | KM=2.4 µM for 4-hydroxypropiophenone (at pH 7.5); | | KM=101 µM for 4-hydroxybenzaldehyde (at pH 8.0); | | KM=0.82 µM for 4-aminoacetophenone (at pH 7.5); | | KM=1.04 mM for 4-fluoroacetophenone (at pH 8.0); | | KM=161 µM for 4-methylacetophenone (at pH 8.0); | | KM=541 µM for 4-methoxyacetophenone (at pH 8.0); | | KM=610 µM for 2-hydroxyacetophenone (at pH 7.5); | | KM=1.4 mM for 3-hydroxyacetophenone (at pH 7.5); | | KM=1.6 mM for benzaldehyde (at pH 7.5); | | KM=2.27 mM for acetophenone (at pH 8.0); | | KM=530 µM for propiophenone (at pH 7.5); | | KM=2 mM for butyrophenone (at pH 7.5); | | KM=540 µM for isobutyrophenone (at pH 7.5); | | KM=1.4 mM for methylphenyl sulfide (at pH 7.5); | | KM=370 µM for methyl 4-tolyl sulfide (at pH 7.5); | | KM=1.2 mM for 2-acetylpyridine (at pH 7.5); | | KM=1.9 mM for 4-acetylpyridine (at pH 7.5); | | KM=330 µM for 2-acetylpyrrole (at pH 7.5); | | KM=410 µM for 2-pyrrole carboxaldehyde (at pH 7.5); | | KM=4.8 mM for acetylcyclohexane (at pH 7.5); | | KM=3 mM for cyclohexane carboxaldehyde (at pH 7.5); | | KM=29 mM for hydroxyacetone (at pH 7.5); | | KM=23 mM for 3-chloro-2-butanone (at pH 7.5); | | KM=4.9 mM for 2,4-pentanedione (at pH 7.5); | | KM=3.3 mM for rac-bicyclo[3.2.0]hept-2-en-6-one (at pH 7.5); | | KM=380 µM for 4-hydroxy-3-methylacetophenone (at pH 8.0); | | pH dependence: |
Optimum pH is 7.5; | | Temperature dependence: |
Optimum temperature is 30 degrees Celsius; | |
- SUBUNIT: Homodimer.
- MASS SPECTROMETRY: Mass=77610; Mass_error=10; Method=Electrospray; Range=2-640; Note=The measured mass is that of a monomer in complex with FAD cofactor; Source=PubMed:16049018;.
- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 640 AA [This is the length of the unprocessed precursor] |
Molecular weight: 71957 Da [This is the MW of the unprocessed precursor] |
CRC64: 60750A318723DA6A [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSAFNTTLPS LDYDDDTLRE HLQGADIPTL LLTVAHLTGD LQILKPNWKP SIAMGVARSG
70 80 90 100 110 120
MDLETEAQVR EFCLQRLIDF RDSGQPAPGR PTSDQLHILG TWLMGPVIEP YLPLIAEEAV
130 140 150 160 170 180
TAEEDLRAPR WHKDHVASGR DFKVVIIGAG ESGMIAALRF KQAGVPFVIY EKGNDVGGTW
190 200 210 220 230 240
RENTYPGCRV DINSFWYSFS FARGIWDDCF APAPQVFAYM QAVAREHGLY EHIRFNTEVS
250 260 270 280 290 300
DAHWDESTQR WQLLYRDSEG QTQVDSNVVV FAVGQLNRPM IPAIPGIETF KGPMFHSAQW
310 320 330 340 350 360
DHDVDWSGKR VGVIGTGASA TQFIPQLAQT AAELKVFART TNWLLPTPDL HEKISDSCKW
370 380 390 400 410 420
LLAHVPHYSL WYRVAMAMPQ SVGFLEDVMV DVGYPPTELA VSARNDRLRQ DISAWMEPQF
430 440 450 460 470 480
ADRPDLREVL IPDSPVGGKR IVRDNGTWIS TLKRDNVSMI RQPIEVITPK GICCVDGTEH
490 500 510 520 530 540
EFDLIVYGTG FHASKFLMPI NVTGRDGVAL HDVWKGDDAR AYLGMTVPQF PNMFCMYGPN
550 560 570 580 590 600
TGLVVYSTVI QFSEMTASYI VDAVRLLLEG GHQSMEVKTP VFESYNQRVD EGNALRAWGF
610 620 630 640
SKVNSWYKNS KGRVTQNFPF TAVEFWQRTH SVEPTDYQLG
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Q93TJ5 in FASTA format |
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