Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The aim of this review is to summarize the data obtained in the author's laboratory during the last decade. The main objects of these investigations were mammalian aminoacyl-tRNA synthetases, mainly bovine tryptophanyl-tRNA synthetase (EC 6.1.1.2). The data are discussed and compared with those described in literature. In the course of these studies it turned out that some properties of mammalian aminoacyl-tRNA synthetases for instance, nuclear location of some of the synthetases, presence of extra-domain in bovine tryptophanyl-tRNA synthetase capable of catalyzing hydrolysis of ATP and GTP in the absence of Zn2+ ions and normal aminoacylation capacity, ability to bind to one of the glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, formation of aminoacylated and pyrophosphorylated forms of tryptophanyl-tRNA synthetase etc., seem to be unrelated to the main function of the synthetases, catalysis of aminoacyl-tRNA formation, and, therefore, might be classified as noncanonical ones. Comparison of prokaryotic and eukaryotic aminoacyl-tRNA synthetases indicates the multipotential nature of the latter.
 ...
PMID:[Aminoacyl-tRNA synthetases (codases) and their noncanonical functions]. 209 4

Bovine tryptophanyl-tRNA synthetase is able to form a complex with glyceraldehyde-3-phosphate dehydrogenase. The complex formation (i) does not influence the tryptophan-dependent PPi-ATP exchange reaction and (ii) involves predominantly the N-terminal dispensable domain of the synthetase. Glyceraldehyde-3-phosphate dehydrogenase was shown to be capable of interacting simultaneously with tryptophanyl-tRNA synthetase and with ribosomal RNA to form a ternary complex. It is proposed that compartmentation of some aminoacyl-tRNA synthetases in certain cases might be achieved via 'adapter' molecules which can bind at once to ribonucleic acids and to aminoacyl-tRNA synthetases.
 ...
PMID:Bovine tryptophanyl-tRNA synthetase and glyceraldehyde-3-phosphate dehydrogenase form a complex. 273 4

Interdomain interactions play an important role in the structural organization of many enzymes and the conformational flexibility of their molecules. In this review, the role of intrasubunit and intersubunit domain-domain interactions in the origins of pre-existent asymmetry of homo-oligomeric D-glyceraldehyde-3-phosphate dehydrogenase and tryptophanyl-tRNA synthetase is discussed on the basis of recent X-ray data and other available information about the properties of these and related enzymes. In addition, a novel key function of interdomain interactions is considered: their potential contribution to intramolecular channeling of intermediates between active centers located on different subunits of a hetero-oligomeric enzyme (alpha,beta-heterodimeric carbamoyl phosphate synthetase).
 ...
PMID:Interdomain interactions in oligomeric enzymes: creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers. 1116 53