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Results 1 - 10 of 12 > >>
EC Number Subunits Commentary Reference
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9? - 529
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9? x * 140000, SDS-PAGE, valyl-tRNA synthetase component purified from the heterotypic complex 528
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9monomer 1 * 100000, SDS-PAGE -, 546
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9monomer 1 * 108000, SDS-PAGE -, 67
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9monomer 1 * 125000, SDS-PAGE -, 529
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9monomer 1 * 126000, urea-SDS-PAGE 434, 537
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9monomer 1 * 140000, SDS-PAGE -, 11, 529, 530
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9monomer the high molecular weight valyl-tRNA synthetase is a homotypic tetramer which converts to the monomeric valyl-tRNA synthetase after cleavage of a small peptide 530
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9More glp-4 VARS-2 has two tRNA recognition domains (1 and 2), a split class 1 Rossmann-fold, which functions in catalyzing the synthesis of aminoacyl-adenylate and aminoacyl-tRNAval, an editing domain, and the connective polypeptide (CP1) domain, which also functions in post-transfer editing. Structural analysis of glp-4 VARS-2, homology modeling, overview 745020
Show all pathways known for 6.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.9More the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview 673963
Results 1 - 10 of 12 > >>