Paul F Fitzpatrick
Overview
Explore the profile of Paul F Fitzpatrick including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
108
Citations
1705
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Fitzpatrick P
Arch Biochem Biophys
. 2024 Nov;
764():110242.
PMID: 39613287
The goals of this presentation are to summarize the present understanding of the mechanism of amine oxidation by flavoproteins and to examine the possibility that a member of the monoamine...
2.
Fitzpatrick P, Daubner S
Methods Enzymol
. 2024 Sep;
704:345-361.
PMID: 39300655
The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase utilize a non-heme iron to catalyze the hydroxylation of the aromatic rings of their amino acid substrates, with...
3.
Fitzpatrick P
Arch Biochem Biophys
. 2023 Jan;
735:109518.
PMID: 36639008
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...
4.
Li M, Subedi B, Fitzpatrick P, Emerson J
Arch Biochem Biophys
. 2022 Aug;
729:109378.
PMID: 35995215
Phenylalanine hydroxylase (PheH) is a pterin-dependent, mononuclear nonheme iron(II) oxygenase that uses the oxidative power of O to hydroxylate phenylalanine to form tyrosine. PheH is a member of a superfamily...
5.
Sies H, Fitzpatrick P, Newman A, Forman H
Arch Biochem Biophys
. 2022 Jun;
726:109295.
PMID: 35752468
No abstract available.
6.
Wanninayake U, Subedi B, Fitzpatrick P
Arch Biochem Biophys
. 2019 Oct;
676:108136.
PMID: 31604072
The flavoprotein trimethylamine dehydrogenase is a member of a small class of flavoproteins that catalyze amine oxidation and transfer the electrons through an Fe/S center to an external oxidant. The...
7.
Fitzpatrick P, Dougherty V, Subedi B, Quilantan J, Hinck C, Lujan A, et al.
Biochemistry
. 2019 May;
58(21):2534-2541.
PMID: 31046245
The flavoprotein d-6-hydroxynicotine oxidase catalyzes an early step in the oxidation of ( R)-nicotine, the oxidation of a carbon-nitrogen bond in the pyrrolidine ring of ( R)-6-hydroxynicotine. The enzyme is...
8.
Khan C, Meisburger S, Ando N, Fitzpatrick P
J Biol Chem
. 2019 Jan;
294(12):4359-4367.
PMID: 30674554
The naturally occurring R68S substitution of phenylalanine hydroxylase (PheH) causes phenylketonuria (PKU). However, the molecular basis for how the R68S variant leads to PKU remains unclear. Kinetic characterization of R68S...
9.
Khan C, Fitzpatrick P
Biochemistry
. 2018 Oct;
57(44):6274-6277.
PMID: 30346142
Liver phenylalanine hydroxylase (PheH) is an allosteric enzyme that is activated by phenylalanine. The enzyme is also phosphorylated by protein kinase A, but the effects of phosphorylation are unclear. Recent...
10.
Fitzpatrick P
Beilstein J Org Chem
. 2018 Sep;
14:2295-2307.
PMID: 30202483
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...