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Results 1 - 8 of 8
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10? N-terminal glutathione S transferase-tagged enzyme, x * 115000, SDS-PAGE 726859
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10? x * 41172, calculation from nucleotide sequence 1396
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10? x * 80759, calculation from nucleotide sequence 1390
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10monomer 1 * 64000, SDS-PAGE 1395
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10monomer 1 * 80759, amino acid sequence calculation 1390
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10monomer 1 * 81000, the two isozymes are monomers both in their apoforms and when bound to the enzymatic intermediate biotinyl 5'-AMP, equilibrium sedimentation centrifugation 704561
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10More modeling of the 3D structure of human HCS, HCS comprises four putative domains, i.e. the N-terminus, the biotin transfer/ATP-binding domain, a putative linker domain, and the C-terminus. Both N- and C-termini are essential for biotinylation of carboxylases by HCS 705752
Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.10More the N-terminal domain has a crucial effect on the enzymatic activity. The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS. It recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain. Human HCS shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus 703738
Results 1 - 8 of 8