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glutamine and IDE

Daniel Morvan, Aicha Demidem
Introduction: Elucidating molecular alterations due to mitochondrial Complex I (CI) mutations may help to understand CI deficiency (CID), not only in mitochondriopathies but also as it is caused by drugs or associated to many diseases. Objectives: CID metabolic expression was investigated in Leber's hereditary optic neuropathy (LHON) caused by an inherited mutation of CI. Methods: NMR-based metabolomics analysis was performed in intact skin fibroblasts from LHON patients...
2018: Metabolomics: Official Journal of the Metabolomic Society
Yan Xiao, Jianqiang Wang, Jun Zhang, Andreas Heise, Meidong Lang
Copolypept(o)ides of polysarcosine (PSar) and poly(N-isopropyl-L-glutamine) (PIGA) with random and block sequence structures were synthesized by ring-opening polymerization (ROP) of sarcosine N-carboxyanhydrides (Sar-NCA) and γ-benzyl-l-glutamate N-carboxyanhydrides (BLG-NCA) and post modification. With different distribution of Sar along the main chain, H-bonding pattern and secondary structure of polypeptides were turned, as well as aggregation and gelation behavior. Both copolypept(o)ides formed hydrogels above their critical gelation concentrations (CGCs) without thermo-sensitivity, which was normally reserved for PEG copolypeptides (eg, PEG-b-PIGA)...
October 2017: Biopolymers
Fernanda Fonseca Botini, Fumie Suzuki-Kemmelmeier, Ecio Alves Nascimento, Luci Tiemi Ide, Adelar Bracht
AIMS/BACKGROUND: Zonation of alanine metabolism was investigated in the bivascularly perfused rat liver, a technique in which a selective area of the periportal region can be reached via the hepatic artery. METHODS: Bivascular liver perfusion was done in both the antegrade and retrograde modes. Predominance of a given metabolic parameter in the periportal or perivenous area was deduced from comparisons of the changes caused by alanine infusion into the hepatic artery in antegrade and retrograde perfusion...
August 2005: Liver International: Official Journal of the International Association for the Study of the Liver
Mads K Dalsgaard, Kojiro Ide, Yan Cai, Bjørn Quistorff, Niels H Secher
During and after maximal exercise there is a 15-30 % decrease in the metabolic uptake ratio (O(2)/[glucose + 1/2 lactate]) and a net lactate uptake by the human brain. This study evaluated if this cerebral metabolic uptake ratio is influenced by the intent to exercise, and whether a change could be explained by substrates other than glucose and lactate. The arterial-internal jugular venous differences (a-v difference) for O(2), glucose and lactate as well as for glutamate, glutamine, alanine, glycerol and free fatty acids were evaluated in 10 healthy human subjects in response to cycling...
April 15, 2002: Journal of Physiology
R K Perlman, B D Gehm, W L Kuo, M R Rosner
Insulin-degrading enzyme (IDE), a nonlysosomal metalloprotease involved in metabolizing internalized insulin, has catalytic properties that have been strongly conserved through evolution. Two major properties distinguish IDE from the prototypic metalloprotease thermolysin. 1) It is inhibited by cysteine protease inhibitors as well as metalloprotease inhibitors; 2) it contains an inversion of the HEXXH active site motif of thermolysin, where the histidines coordinate zinc and the glutamate participates in catalysis...
October 15, 1993: Journal of Biological Chemistry
T Kanaji, H Ozaki, T Takao, H Kawajiri, H Ide, M Motoki, Y Shimonishi
The complete amino acid sequence of transglutaminase (EC (TGase), which is produced by a microorganism, Streptoverticillium sp. strain s-8112, and catalyzes the acyl transfer reaction between gamma-carboxyamide groups of glutamine residues in proteins and various primary amines, has been established by a combination of fast atom bombardment mass spectrometry and standard Edman degradation of peptide fragments produced by treatment of the TGase with various proteolytic enzymes and purified by a reversed-phase high performance liquid chromatography...
June 5, 1993: Journal of Biological Chemistry
R K Perlman, M R Rosner
The insulin degrading enzyme (IDE), a nonlysosomal enzyme involved in the metabolism of internalized insulin, is a member of a new family of metalloproteases which has an HXXEH active site motif. We have previously shown that both His108 and Glu111 within the HXCEH domain of human IDE are necessary for catalytic activity. Comparison to the prototypic zinc metalloprotease thermolysin, which contains an inversion of this motif, would predict that His112, as well as a downstream glutamate, serves as the second and third zinc ligands of IDE...
December 30, 1994: Journal of Biological Chemistry
Y Ide, H Matsumoto
No abstract text is available yet for this article.
April 1977: Nihon Juigaku Zasshi. the Japanese Journal of Veterinary Science
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