Results 61 to 70 of about 104,062 (224)

Structural basis of autoregulation of phenylalanine hydroxylase

open access: yes, 1999
Phenylalanine hydroxylase converts phenylalanine to tyrosine, a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis.
Goodwill, KE   +8 more
core   +1 more source

Simultaneous Overexpression of FERULOYL‐CoA 6′‐HYDROXYLASE 1 and COUMARIN SYNTHASE Leads to Coumarin‐Enriched Lignin and Improved Saccharification in Greenhouse‐ and Field‐Grown Poplar

open access: yesPlant Biotechnology Journal, EarlyView.
ABSTRACT The urgent need for renewable resources has increased the interest in woody biomass to manufacture bio‐based products. However, lignin recalcitrance limits the enzymatic conversion of wood into fermentable sugars, posing a major challenge for biomass deconstruction.
Nette De Ridder   +9 more
wiley   +1 more source

Aminopeptidase C of Aspergillus niger is a Novel Phenylalanine Aminopeptidase [PDF]

open access: yes, 2003
A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share ...
Dekker, P.J.T.   +2 more
core   +1 more source

Mutation analysis of Phenylalanine hydroxylase gene in Iranian patients with Phenylketonuria. [PDF]

open access: yesMed J Islam Repub Iran, 2018
Background: Phenylketonuria as the most common genetic metabolic disorder is the result of disruption of the phenylalanine hydroxylase gene.
Rastegar Moghadam M   +4 more
europepmc   +2 more sources

Unexpected Suppression of Tomato Fruit Cuticle Formation by Overexpression of a Key Cutin Biosynthetic Enzyme

open access: yesPlant Biotechnology Journal, EarlyView.
ABSTRACT Fruit cuticles regulate the diffusion of water, gases and solutes, functioning as essential protective interfaces against environmental and biotic stresses. Engineering cuticle structure and mechanics therefore represents a promising strategy for improving fruit quality and resilience.
Gulab Chand Arya   +5 more
wiley   +1 more source

Mutation Analysis of PAH Gene in Phenylketonuria Patients from the North of Iran: Identification of Three Novel Pathogenic Variants

open access: yesInternational Journal of Preventive Medicine
Background: There are more than 1100 different pathogenic variants in the phenylalanine hydroxylase (PAH) gene that are responsible for phenylketonuria (PKU) diseases, and the spectrum of these mutations varies in different ethnic groups.
Hossein Jalali   +5 more
doaj   +1 more source

SbWRKY62 Coordinates With SbERF096 to Activate Pterostilbene Biosynthesis and Targets a Xylanase Inhibitor Protein for Anthracnose Resistance in Sorghum

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Sorghum anthracnose caused by Colletotrichum sublineola (C. sublineola) is a destructive disease leading to severe crop damages. Pterostilbene is a phytoalexin that contributes to defence responses in sorghum, but the transcriptional regulation of its biosynthesis remained poorly understood.
Yajing Li   +5 more
wiley   +1 more source

Chronic Immune Stimulation May Cause Moderate Impairment of Phenylalanine 4-hydroxylase

open access: yesPteridines, 2011
Phenylalanine (4)-hydroxylase (PAH, E.C. 1.14.16.1) is located mainly in liver and converts amino acid phenylalanine (Phe) to tyrosine (Tyr). In 'classical' phenylketonuria (PKU), PAH activity is reduced, whereas in 'atypical' PKU biosynthesis of the ...
Scholl-Bürgi S   +4 more
doaj   +1 more source

Biopterin responsive phenylalanine hydroxylase deficiency [PDF]

open access: yesGenetics in Medicine, 2004
Phenylketonuria (PKU) is an autosomal recessive disorder caused by mutations in the phenylalanine hydroxylase (PAH) gene. There have been more than 400 mutations identified in the PAH gene leading to variable degrees of deficiency in PAH activity, and consequently a wide spectrum of clinical severity.
Reuben, Matalon   +11 more
openaire   +2 more sources

Molecular dynamics simulation data of rat phenylalanine hydroxylase (rPAH) tetramer

open access: yes, 2020
Raw data of molecular dynamics simulations of rat phenylalanine hydroxylase (T22-K450) tetramer. Missing residues were rebuilt using Modeller. Metal site was parameterized using MCPB.py in AmberTools. Simulation starts from the crystal pose (PDB: 5DEN)
Ge Yunhui, Voelz Vincent
core   +1 more source

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