Results 181 to 190 of about 3,274 (204)

Nucleotide sequence of a cDNA encoding murine fumarylacetoacetate hydrolase

Biochemical Medicine and Metabolic Biology, 1992
Hereditary tyrosinemia type I is caused by deficiency of the enzyme fumarylacetoacetate hydrolase (FAH) (EC 3.7.1.2), the final step in tyrosine degradation. We report here the cloning and sequencing of a full length cDNA coding for murine FAH. This cDNA is highly homologous to the previously cloned human and rat genes.
Markus Grompe
exaly   +3 more sources

X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880

Biological Chemistry, 2004
Abstract The human protein FLJ36880 belongs to the fumarylacetoacetate hydrolase family. The X-ray structure of FLJ36880 has been determined to 2.2 Å resolution employing the semi-automated high-throughput structural genomics approach of the Protein Structure Factory.
Babu A Manjasetty, Udo Heinemann
exaly   +4 more sources

Fumarylacetoacetate hydrolase is involved in salt stress response in Arabidopsis

Planta, 2018
Fumarylacetoacetate hydrolase participates in positive regulation of salt stress in Arabidopsis. Fumarylacetoacetate hydrolase (FAH) catalyzes the hydrolysis of fumarylacetoacetate into fumarate and acetoacetate, the final step in the Tyr degradation pathway that is essential to animals.
Lihua Huang, Chao Hu, Wei Cai, Qi Zhu, Bida Gao, Xuewen Zhang, Chunmei Ren   +6 more
openaire   +2 more sources

Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum

Biochemical and Biophysical Research Communications, 2019
Fumarylacetoacetate hydrolase (FAH) is essential for the degradation of aromatic amino acids as well as for the cleavage of carbon-carbon bonds in metabolites or small organic compounds. Here, the X-ray crystal structure of EaFAH, a dimeric fumarylacetoacetate hydrolase from Exiguobacterium antarcticum, was determined, and its functional properties ...
Wanki Yoo, Han-Woo Kim, Kyeong Kyu Kim
exaly   +3 more sources

Fumarylacetoacetate Hydrolase Deficiency

2009
Robert J. Desnick, Orlando Guntinas-Lichius, George W. Padberg, Gustav Schonfeld, Xiaobo Lin, Maurizio Averna, Pin Yue, John-John B. Schnog, Victor E. A. Gerdes, Pedro R. Cutillas, Robert J. Unwin, Heike Schulze, Konrad Sandhoff, Jean-François Pellissier, Georges Serratrice, Dominique Figarella-Branger, Cord Sunderkötter, Marcelo Gustavo Binker, Laura Iris Cosen-Binker, Matthias Wettstein, Peter von den Driesch, Rima Nabbout, Massimo Mantegazza, Olivier Dulac, Johann Michael Schröder, Ho Sung Kang, Johann Michael Schröder, Marina Marchetti Hugo Ten Cate, Marina Marchetti, Hugo ten Cate, Lev I. Patrushev, Lee S. Weinstein, Adiba Isa, Fernando Azpiroz, Guang-Sheng Li, Ling Jing, Hui Xu, Anne M. Molloy, John M. Scott, Cord Sunderkötter, Axel Lorentz, Stephan C. Bischoff, Filippo Tamanini, Filippo Tamanini, Thomas Klockgether, Derek A. Wong, Jürgen Kopitz, Carolina von Reitzenstein, Michael Cantz   +48 more
exaly   +2 more sources

Sugar suppresses cell death caused by disruption of fumarylacetoacetate hydrolase in Arabidopsis

Planta, 2016
Sugar negatively regulates cell death resulting from the loss of fumarylacetoacetate hydrolase that catalyzes the last step in the Tyr degradation pathway in Arabidopsis . Fumarylacetoacetate hydrolase (FAH) hydrolyzes fumarylacetoacetate to fumarate and acetoacetate, the final step in the tyrosine (Tyr) degradation pathway that is essential to animals.
Tiantian, Zhi, Zhou, Zhou, Yi, Huang, Chengyun, Han, Yan, Liu, Qi, Zhu, Chunmei, Ren   +6 more
openaire   +2 more sources

The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes: multifunctional enzymes from microbes to mitochondria

Biochemical Society Transactions, 2018
Prokaryotic and eukaryotic fumarylacetoacetate hydrolase (FAH) superfamily members, sharing conserved regions that form the so-called FAH-domain, catalyze a remarkable variety of reactions. These enzymes are essential in the metabolic pathways to degrade aromatic compounds in prokaryotes and eukaryotes.
Weiss, Alexander K. H., Loeffler, Johannes R., Liedl, Klaus R., Gstach, Hubert, Jansen-Duerr, Pidder   +4 more
openaire   +3 more sources

Mutations of the fumarylacetoacetate hydrolase gene in four patients with tyrosinemia, type I

Human Mutation, 1993
Tyrosinemia type I is an autosomal recessive inborn error of metabolism caused by deficiency of the enzyme fumaryl acetoacetate hydrolase (FAH, EC 3.7.1.2). We have used reverse transcription and the polymerize chain reaction to amplify the peptide coding region of the FAH cDNA from four patients with tyrosinemia type I.
M, Grompe, M, al-Dhalimy
openaire   +2 more sources

Purification of mRNA coding for the enzyme deficient in hereditary tyrosinemia, fumarylacetoacetate hydrolase

Biochemistry and Cell Biology, 1986
As a step towards the cloning of the gene for fumarylacetoacetate hydrolase (FAH), we have purified the FAH mRNA from rat liver by specific immunoadsorption of polysomes. The relative abundance of this mRNA has been estimated to be 0.14%. The major in vitro translation product of the purified mRNA preparation is specifically precipitated by a rabbit ...
L M, Nicole, J P, Valet, C, Laberge, R M, Tanguay   +3 more
openaire   +2 more sources

Structural organization and analysis of the human fumarylacetoacetate hydrolase gene in tyrosinemia type I

Biochimica Et Biophysica Acta - Molecular Basis of Disease, 1994
Fumarylacetoacetate hydrolase (FAH) is a metabolic enzyme functioning at the last step of tyrosine catabolism. Deficiency in this enzyme activity is associated with tyrosinemia type I, characterized by hypertyrosinemia, liver dysfunction, renal tubular dysfunction, liver cirrhosis, and hepatic tumors. We isolated from a human gene library a chromosomal
H, Awata, F, Endo, A, Tanoue, A, Kitano, Y, Nakano, I, Matsuda   +5 more
exaly   +3 more sources