Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster.
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Genome-guided analysis of physiological and morphological traits of the fermentative acetate oxidizer Thermacetogenium phaeumTetrahydrobiopterin biosynthesis, regeneration and functionsStudies on the enzymatic and transcriptional activity of the dimerization cofactor for hepatocyte nuclear factor 1The TyrA family of aromatic-pathway dehydrogenases in phylogenetic contextStructure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stabilitySolution NMR structures of proteins VPA0419 fromVibrio parahaemolyticusand yiiS fromShigella flexneriprovide structural coverage for protein domain family PFAM 04175Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1Characterization of the wild-type form of 4a-carbinolamine dehydratase and two naturally occurring mutants associated with hyperphenylalaninemiaFolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosaThe homogentisate pathway: a central catabolic pathway involved in the degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in Pseudomonas putida.Functional identification of orthologous genes encoding pterin recycling activity in Plasmodium falciparum and Toxoplasma gondiiMetabolic reconstruction of aromatic compounds degradation from the genome of the amazing pollutant-degrading bacterium Cupriavidus necator JMP134.Genetic characterization of the major lactococcal aromatic aminotransferase and its involvement in conversion of amino acids to aroma compounds.Chlamydia pneumoniae encodes a functional aromatic amino acid hydroxylase.Phenylalanine hydroxylase (PAH) from the lower eukaryote Leishmania major.Phenylalanine hydroxylase from Legionella pneumophila is a thermostable enzyme with a major functional role in pyomelanin synthesis.Interactions with the bifunctional interface of the transcriptional coactivator DCoH1 are kinetically regulated.Identification and molecular characterization of the homogentisate pathway responsible for pyomelanin production, the major melanin constituents in Aeromonas media WSEvolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases.Identification of hepatic nuclear factor 1 binding sites in the 5' flanking region of the human phenylalanine hydroxylase gene: implication of a dual function of phenylalanine hydroxylase stimulator in the phenylalanine hydroxylation system.Osmoregulation in the Halophilic Bacterium Halomonas elongata: A Case Study for Integrative Systems Biology.The ins and outs of ring-cleaving dioxygenases.Delineation of the arginine- and tetrahydrobiopterin-binding sites of neuronal nitric oxide synthase.Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli.Role of the phenylalanine-hydroxylating system in aromatic substance degradation and lipid metabolism in the oleaginous fungus Mortierella alpinaDisruption of phenylalanine hydroxylase reduces adult lifespan and fecundity, and impairs embryonic development in parthenogenetic pea aphidsEndophytic Bacterium Pseudomonas fluorescens RG11 May Transform Tryptophan to Melatonin and Promote Endogenous Melatonin Levels in the Roots of Four Grape Cultivars.Phenylalanine hydroxylase: function, structure, and regulation.PhhB, a Pseudomonas aeruginosa homolog of mammalian pterin 4a-carbinolamine dehydratase/DCoH, does not regulate expression of phenylalanine hydroxylase at the transcriptional levelEnhanced synthesis of 5-hydroxy-l-tryptophan through tetrahydropterin regeneration.Structure and function of the aromatic amino acid hydroxylases.Dihydropteridine reductase as an alternative to dihydrofolate reductase for synthesis of tetrahydrofolate in Thermus thermophilus.Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogueL-Arogenate Is a Chemoattractant Which Can Be Utilized as the Sole Source of Carbon and Nitrogen by Pseudomonas aeruginosa.Functional analysis of aromatic biosynthetic pathways in Pseudomonas putida KT2440.Nonflowering plants possess a unique folate-dependent phenylalanine hydroxylase that is localized in chloroplasts.Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: recurrence of tyrosine aminotransferase activity in the Iα subfamily.Phylogenomic and functional analysis of pterin-4a-carbinolamine dehydratase family (COG2154) proteins in plants and microorganisms.Pterin and folate salvage. Plants and Escherichia coli lack capacity to reduce oxidized pterins.
P2860
Q21266685-27C12E84-AB75-404E-9A3C-4B80C59AA67FQ24531994-F002E4AD-157C-49C0-BDAB-FC93CF7D4F2BQ24633231-D524AE1F-8DA8-4ACA-877D-370723C85F43Q24815474-1DC6CBB1-E1D4-47C7-ABE5-CE2817C9BF23Q27645041-5E44FB30-454D-40F7-81ED-E69A99E18F03Q27658281-261D045E-0238-403B-B53A-60D80304201FQ28115243-5BEC9E65-8F8D-4DC5-A555-B83D99AB7782Q28277309-3B0ACDDD-F4F9-4FD9-A3CE-C745996BAD1FQ28493203-4BBCE741-DB53-41A3-A75A-DAC208D3F0DBQ29346848-E315C00E-5399-4961-8ADD-0D68621B6465Q33228901-EA2180BE-96F9-4237-980C-BEC16D1CCC8FQ33358902-D9523B63-89D9-40D9-9FD2-9C5ACD574434Q33985964-182ECD0D-5140-414B-A68C-7DE30F9C1498Q34066394-F9F44F4E-4A79-4C60-92D2-E3FE20806E07Q34328735-4182D297-24FA-482A-BB01-601A691D1476Q34438667-EFBAFBF0-E5EB-4C1B-9B6C-D71712165B97Q35080345-5E8F4D5D-6AA7-45FA-987C-64E9286AAD2AQ35202289-A0AF8E76-A51B-4CE0-9B86-C9794A0866CEQ35605169-9EB36A7D-2207-4F60-8E36-0C107EF6E193Q35868114-F0FABDC4-F86D-41CD-BAAD-ADD90BACFADCQ36247513-C0D209DF-7BC7-4A58-AF40-4DB0E8255F6CQ36539821-4218829B-FB3B-46B1-8DE2-83F8ECF49A97Q36863994-9388E9D4-46A2-4BFD-8EF8-2A9E0145683CQ36865251-88501FCF-90D8-4AEF-B6CE-67C2863FAA7AQ36936418-C3CA5934-C390-40D6-897D-62839F8E8837Q37303519-CF48D9E1-0689-4E94-B21A-C675CD2F87F9Q37575584-3D35604C-DEB8-4118-9293-D1C6D82F945EQ38086186-5F6D6685-B7A6-4C49-AE62-16CC39C6C571Q39495505-6160EBB7-D37D-4323-A8D0-362EA4A3EC77Q39829968-70D3ED45-4F56-4415-A8B7-CCF9DBB24DEDQ40375232-B892238A-6940-449E-864A-586FDAD4AC57Q40387760-CB79A58A-54E5-4F0E-A18D-BABEF40F6F34Q41817640-B775C5C7-E8F2-450F-9CFF-881005A21F04Q42015563-A5BCBF0B-F2D7-4E1C-94A1-BD7609582D83Q42096032-54D86E58-B34F-49E0-A99D-9EA5C18E0E5BQ42755380-FAF40A23-7023-4EF1-AE7D-AACF4BFE2892Q42853992-D3C52425-3CE8-4CA8-AF17-42D3021EF981Q42914294-5060BF94-20AF-40C8-897E-1318445E27E3Q46775326-9BCEAA8B-23ED-4246-BA18-DFBD58152509Q54448598-9538D491-4C52-4A9B-A794-A35544606E75
P2860
Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster.
description
1994 nî lūn-bûn
@nan
1994 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Pseudomonas aeruginosa possess ...... three-component gene cluster.
@en
type
label
Pseudomonas aeruginosa possess ...... three-component gene cluster.
@en
prefLabel
Pseudomonas aeruginosa possess ...... three-component gene cluster.
@en
P2093
P2860
P356
P1476
Pseudomonas aeruginosa possess ...... three-component gene cluster.
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.4.1366
P407
P577
1994-02-01T00:00:00Z