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  1. Article ; Online: The aromatic amino acid hydroxylases: Structures, catalysis, and regulation of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase.

    Fitzpatrick, Paul F

    Archives of biochemistry and biophysics

    2023  Volume 735, Page(s) 109518

    Abstract: The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase are non-heme iron enzymes that catalyze key physiological reactions. This review discusses the present understanding of the common catalytic ... ...

    Abstract The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase are non-heme iron enzymes that catalyze key physiological reactions. This review discusses the present understanding of the common catalytic mechanism of these enzymes and recent advances in understanding the relationship between their structures and their regulation.
    MeSH term(s) Mixed Function Oxygenases/chemistry ; Tryptophan Hydroxylase/chemistry ; Tryptophan Hydroxylase/metabolism ; Tyrosine 3-Monooxygenase/chemistry ; Tyrosine 3-Monooxygenase/metabolism ; Phenylalanine Hydroxylase/chemistry ; Phenylalanine Hydroxylase/metabolism ; Amino Acids, Aromatic ; Catalysis
    Chemical Substances Mixed Function Oxygenases (EC 1.-) ; Tryptophan Hydroxylase (EC 1.14.16.4) ; Tyrosine 3-Monooxygenase (EC 1.14.16.2) ; Phenylalanine Hydroxylase (EC 1.14.16.1) ; Amino Acids, Aromatic
    Language English
    Publishing date 2023-01-10
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2023.109518
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  2. Article: The enzymes of microbial nicotine metabolism.

    Fitzpatrick, Paul F

    Beilstein journal of organic chemistry

    2018  Volume 14, Page(s) 2295–2307

    Abstract: Because of nicotine's toxicity and the high levels found in tobacco and in the waste from tobacco processing, there is a great deal of interest in identifying bacteria capable of degrading it. A number of microbial pathways have been identified for ... ...

    Abstract Because of nicotine's toxicity and the high levels found in tobacco and in the waste from tobacco processing, there is a great deal of interest in identifying bacteria capable of degrading it. A number of microbial pathways have been identified for nicotine degradation. The first and best-understood is the pyridine pathway, best characterized for
    Language English
    Publishing date 2018-08-31
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 2192461-2
    ISSN 1860-5397
    ISSN 1860-5397
    DOI 10.3762/bjoc.14.204
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  3. Article ; Online: Nitroalkane oxidase: Structure and mechanism.

    Fitzpatrick, Paul F

    Archives of biochemistry and biophysics

    2017  Volume 632, Page(s) 41–46

    Abstract: The flavoprotein nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to the corresponding aldehydes or ketones, releasing nitrite and transferring electrons to ... ...

    Abstract The flavoprotein nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to the corresponding aldehydes or ketones, releasing nitrite and transferring electrons to O
    MeSH term(s) Aldehydes/chemistry ; Aldehydes/metabolism ; Catalysis ; Dioxygenases/chemistry ; Dioxygenases/metabolism ; Electron Transport ; Flavoproteins/chemistry ; Flavoproteins/metabolism ; Hydrogen Peroxide/chemistry ; Hydrogen Peroxide/metabolism ; Ketones/chemistry ; Ketones/metabolism ; Nitrites/chemistry ; Nitrites/metabolism ; Oxygen/chemistry ; Oxygen/metabolism ; Structure-Activity Relationship
    Chemical Substances Aldehydes ; Flavoproteins ; Ketones ; Nitrites ; Hydrogen Peroxide (BBX060AN9V) ; Dioxygenases (EC 1.13.11.-) ; 2-nitropropane dioxygenase (EC 1.13.12.16) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2017-05-18
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2017.05.012
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  4. Article ; Online: Archives of Biochemistry and Biophysics: 80th Anniversary.

    Sies, Helmut / Fitzpatrick, Paul F / Newman, Anthony / Forman, Henry Jay

    Archives of biochemistry and biophysics

    2022  Volume 726, Page(s) 109295

    MeSH term(s) Anniversaries and Special Events ; Biochemistry ; Biophysics ; History, 20th Century
    Language English
    Publishing date 2022-06-22
    Publishing country United States
    Document type Editorial ; Historical Article
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2022.109295
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  5. Article ; Online: Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum.

    Li, Mingjie / Subedi, Bishnu P / Fitzpatrick, Paul F / Emerson, Joseph P

    Archives of biochemistry and biophysics

    2022  Volume 729, Page(s) 109378

    Abstract: Phenylalanine hydroxylase (PheH) is a pterin-dependent, mononuclear nonheme iron(II) oxygenase that uses the oxidative power of ... ...

    Abstract Phenylalanine hydroxylase (PheH) is a pterin-dependent, mononuclear nonheme iron(II) oxygenase that uses the oxidative power of O
    MeSH term(s) Biopterins/analogs & derivatives ; Chromobacterium ; Ferrous Compounds ; Iron/metabolism ; Kinetics ; Metalloproteins/metabolism ; Phenylalanine/metabolism ; Phenylalanine Hydroxylase/chemistry ; Phenylalanine Hydroxylase/metabolism ; Pterins/chemistry ; Pterins/metabolism ; Thermodynamics ; Tyrosine
    Chemical Substances Ferrous Compounds ; Metalloproteins ; Pterins ; Biopterins ; Tyrosine (42HK56048U) ; Phenylalanine (47E5O17Y3R) ; Iron (E1UOL152H7) ; Phenylalanine Hydroxylase (EC 1.14.16.1) ; sapropterin (EGX657432I)
    Language English
    Publishing date 2022-08-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2022.109378
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  6. Article ; Online: The enzymes of microbial nicotine metabolism

    Paul F. Fitzpatrick

    Beilstein Journal of Organic Chemistry, Vol 14, Iss 1, Pp 2295-

    2018  Volume 2307

    Abstract: Because of nicotine’s toxicity and the high levels found in tobacco and in the waste from tobacco processing, there is a great deal of interest in identifying bacteria capable of degrading it. A number of microbial pathways have been identified for ... ...

    Abstract Because of nicotine’s toxicity and the high levels found in tobacco and in the waste from tobacco processing, there is a great deal of interest in identifying bacteria capable of degrading it. A number of microbial pathways have been identified for nicotine degradation. The first and best-understood is the pyridine pathway, best characterized for Arthrobacter nicotinovorans, in which the first reaction is hydroxylation of the pyridine ring. The pyrrolidine pathway, which begins with oxidation of a carbon–nitrogen bond in the pyrrolidine ring, was subsequently characterized in a number of pseudomonads. Most recently, a hybrid pathway has been described, which incorporates the early steps in the pyridine pathway and ends with steps in the pyrrolidine pathway. This review summarizes the present status of our understanding of these pathways, focusing on what is known about the individual enzymes involved.
    Keywords biodegradation ; enzyme mechanism ; flavoprotein ; metabolic pathway ; nicotine ; Science ; Q ; Organic chemistry ; QD241-441
    Subject code 570
    Language English
    Publishing date 2018-08-01T00:00:00Z
    Publisher Beilstein-Institut
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: Combining solvent isotope effects with substrate isotope effects in mechanistic studies of alcohol and amine oxidation by enzymes.

    Fitzpatrick, Paul F

    Biochimica et biophysica acta

    2015  Volume 1854, Issue 11, Page(s) 1746–1755

    Abstract: Oxidation of alcohols and amines is catalyzed by multiple families of flavin- and pyridine nucleotide-dependent enzymes. Measurement of solvent isotope effects provides a unique mechanistic probe of the timing of the cleavage of the OH and NH bonds, ... ...

    Abstract Oxidation of alcohols and amines is catalyzed by multiple families of flavin- and pyridine nucleotide-dependent enzymes. Measurement of solvent isotope effects provides a unique mechanistic probe of the timing of the cleavage of the OH and NH bonds, necessary information for a complete description of the catalytic mechanism. The inherent ambiguities in interpretation of solvent isotope effects can be significantly decreased if isotope effects arising from isotopically labeled substrates are measured in combination with solvent isotope effects. The application of combined solvent and substrate (mainly deuterium) isotope effects to multiple enzymes is described here to illustrate the range of mechanistic insights that such an approach can provide. This article is part of a Special Issue entitled: Enzyme Transition States from Theory and Experiment.
    MeSH term(s) Alcohols/chemistry ; Alcohols/metabolism ; Amines/chemistry ; Amines/metabolism ; Biocatalysis ; Deuterium/chemistry ; Enzymes/chemistry ; Enzymes/metabolism ; Isotopes/chemistry ; Models, Chemical ; Molecular Structure ; Solvents/chemistry ; Substrate Specificity
    Chemical Substances Alcohols ; Amines ; Enzymes ; Isotopes ; Solvents ; Deuterium (AR09D82C7G)
    Language English
    Publishing date 2015-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbapap.2014.10.020
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  8. Article ; Online: Structural insights into the regulation of aromatic amino acid hydroxylation.

    Fitzpatrick, Paul F

    Current opinion in structural biology

    2015  Volume 35, Page(s) 1–6

    Abstract: The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase are homotetramers, with each subunit containing a homologous catalytic domain and a divergent regulatory domain. The solution structure of ... ...

    Abstract The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase are homotetramers, with each subunit containing a homologous catalytic domain and a divergent regulatory domain. The solution structure of the regulatory domain of tyrosine hydroxylase establishes that it contains a core ACT domain similar to that in phenylalanine hydroxylase. The isolated regulatory domain of tyrosine hydroxylase forms a stable dimer, while that of phenylalanine hydroxylase undergoes a monomer-dimer equilibrium, with phenylalanine stabilizing the dimer. These solution properties are consistent with the regulatory mechanisms of the two enzymes, in that phenylalanine hydroxylase is activated by phenylalanine binding to an allosteric site, while tyrosine hydroxylase is regulated by binding of catecholamines in the active site.
    MeSH term(s) Amino Acid Sequence ; Amino Acids, Aromatic/metabolism ; Humans ; Hydroxylation ; Mixed Function Oxygenases/chemistry ; Mixed Function Oxygenases/metabolism ; Molecular Sequence Data ; Protein Multimerization
    Chemical Substances Amino Acids, Aromatic ; Mixed Function Oxygenases (EC 1.-)
    Language English
    Publishing date 2015-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2015.07.004
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  9. Article ; Online: Mutagenesis of an Active-Site Loop in Tryptophan Hydroxylase Dramatically Slows the Formation of an Early Intermediate in Catalysis.

    Subedi, Bishnu P / Fitzpatrick, Paul F

    Journal of the American Chemical Society

    2018  Volume 140, Issue 15, Page(s) 5185–5192

    Abstract: Solution studies of the aromatic amino acid hydroxylases are consistent with the ... ...

    Abstract Solution studies of the aromatic amino acid hydroxylases are consistent with the Fe
    Language English
    Publishing date 2018--18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.8b00936
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  10. Article: Nitroalkane oxidase: Structure and mechanism

    Fitzpatrick, Paul F

    Archives of biochemistry and biophysics. 2017,

    2017  

    Abstract: The flavoprotein nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to the corresponding aldehydes or ketones, releasing nitrite and transferring electrons to O2 to form H2O2. A combination of solution and structural analyses have ... ...

    Abstract The flavoprotein nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to the corresponding aldehydes or ketones, releasing nitrite and transferring electrons to O2 to form H2O2. A combination of solution and structural analyses have provided a detailed understanding of the mechanism of this enzyme.
    Keywords aldehydes ; electrons ; flavoproteins ; hydrogen peroxide ; ketones ; nitrites ; oxidation ; oxygen
    Language English
    Size p. .
    Publishing place Elsevier Inc.
    Document type Article
    Note Pre-press version
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2017.05.012
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