نتایج جستجو برای: proline dehydrogenase prodh

تعداد نتایج: 87736  

2016
C L Clelland V Drouet K C Rilett J A Smeed R H Nadrich A Rajparia L L Read J D Clelland

Elevated peripheral proline is associated with psychiatric disorders, and there is evidence that proline is a neuromodulator. The proline dehydrogenase (PRODH) gene, which encodes the enzyme that catalyzes proline catabolism, maps to human chromosome 22q11.2, a region conferring risk of schizophrenia. In the Prodh-null mouse, an interaction between elevated peripheral proline and another 22q11....

Journal: : 2023

Aim. Production of genetically modified plants new promising winter wheat genotypes with partial suppression the proline dehydrogenase gene in vitro culture and determination content transgenic control plants. Methods. Agrobacterium-mediated transformation vitro, molecular genetic analysis; biochemical content; mathematical statistics. Results. Using method callus cultures wheat, carrying a dou...

Journal: :The EMBO journal 2006
Fridtjof Weltmeier Andrea Ehlert Caroline S Mayer Katrin Dietrich Xuan Wang Katia Schütze Rosario Alonso Klaus Harter Jesús Vicente-Carbajosa Wolfgang Dröge-Laser

Proline metabolism has been implicated in plant responses to abiotic stresses. The Arabidopsis thaliana proline dehydrogenase (ProDH) is catalysing the first step in proline degradation. Transcriptional activation of ProDH by hypo-osmolarity is mediated by an ACTCAT cis element, a typical binding site of basic leucine zipper (bZIP) transcription factors. In this study, we demonstrate by gain-of...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Dhiraj Srivastava Jonathan P Schuermann Tommi A White Navasona Krishnan Nikhilesh Sanyal Greg L Hura Anmin Tan Michael T Henzl Donald F Becker John J Tanner

The bifunctional proline catabolic flavoenzyme, proline utilization A (PutA), catalyzes the oxidation of proline to glutamate via the sequential activities of FAD-dependent proline dehydrogenase (PRODH) and NAD(+)-dependent Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) domains. Although structures for some of the domains of PutA are known, a structure for the full-length protein has no...

Journal: :Human molecular genetics 2007
Grégory Raux Emilie Bumsel Bernadette Hecketsweiler Therese van Amelsvoort Janneke Zinkstok Sylvie Manouvrier-Hanu Carole Fantini Georges-Marie M Brévière Gabriella Di Rosa Giuseppina Pustorino Annick Vogels Ann Swillen Solenn Legallic Jacqueline Bou Gaelle Opolczynski Valérie Drouin-Garraud Marie Lemarchand Nicole Philip Aude Gérard-Desplanches Michèle Carlier Anne Philippe Marie Christine Nolen Delphine Heron Pierre Sarda Didier Lacombe Cyril Coizet Yves Alembik Valérie Layet Alexandra Afenjar Didier Hannequin Caroline Demily Michel Petit Florence Thibaut Thierry Frebourg Dominique Campion

Microdeletions of the 22q11 region, responsible for the velo-cardio-facial syndrome (VCFS), are associated with an increased risk for psychosis and mental retardation. Recently, it has been shown in a hyperprolinemic mouse model that an interaction between two genes localized in the hemideleted region, proline dehydrogenase (PRODH) and catechol-o-methyl-transferase (COMT), could be involved in ...

Journal: :The Journal of biological chemistry 2009
Gad Miller Arik Honig Hanan Stein Nobuhiro Suzuki Ron Mittler Aviah Zilberstein

The two-step oxidation of proline in all eukaryotes is performed at the inner mitochondrial membrane by the consecutive action of proline dehydrogenase (ProDH) that produces Delta(1)-pyrroline-5-carboxylate (P5C) and P5C dehydrogenase (P5CDH) that oxidizes P5C to glutamate. This catabolic route is down-regulated in plants during osmotic stress, allowing free Pro accumulation. We show here that ...

Journal: :Molecules 2018
Mieke M E Huijbers Ilona van Alen Jenny W Wu Arjan Barendregt Albert J R Heck Willem J H van Berkel

Proline dehydrogenase (ProDH) is a ubiquitous flavoenzyme that catalyzes the oxidation of proline to Δ¹-pyrroline-5-carboxylate. Thermus thermophilus ProDH (TtProDH) contains in addition to its flavin-binding domain an N-terminal arm, consisting of helices αA, αB, and αC. Here, we report the biochemical properties of the helical arm truncated TtProDH variants ΔA, ΔAB, and ΔABC, produced with ma...

2016
Nikhilesh Sanyal Donald F. Becker

In cell metabolism, substrate channeling is a phenomenon where the product of one reaction is transported to a second enzyme active site without equilibrating into bulk solvent. Chapter 1 reviews the rationale and evidence for substrate channeling with the specific example of proline metabolism. Oxidation of proline to glutamate is catalyzed in consecutive reactions by proline dehydrogenase (PR...

Journal: :Plant physiology 2002
Rie Satoh Kazuo Nakashima Motoaki Seki Kazuo Shinozaki Kazuko Yamaguchi-Shinozaki

Proline (Pro) is one of the most widely distributed osmolytes in water-stressed plants. We previously isolated from Arabidopsis a gene encoding Pro dehydrogenase (ProDH), a mitochondrial enzyme involved in the first step of the conversion of Pro to glutamic acid. The ProDH gene in Arabidopsis is up-regulated by rehydration after dehydration but is down-regulated by dehydration. ProDH is also in...

Journal: :Biochemistry 2017
Shelbi L Christgen Weidong Zhu Nikhilesh Sanyal Bushra Bibi John J Tanner Donald F Becker

Escherichia coli proline utilization A (EcPutA) is the archetype of trifunctional PutA flavoproteins, which function both as regulators of the proline utilization operon and bifunctional enzymes that catalyze the four-electron oxidation of proline to glutamate. EcPutA shifts from a self-regulating transcriptional repressor to a bifunctional enzyme in a process known as functional switching. The...

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