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Results 1 - 8 of 8
EC Number
Subunits
Commentary
Reference
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N-terminal glutathione S transferase-tagged enzyme, x * 115000, SDS-PAGE
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x * 41172, calculation from nucleotide sequence
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x * 80759, calculation from nucleotide sequence
monomer
1 * 64000, SDS-PAGE
monomer
1 * 80759, amino acid sequence calculation
monomer
1 * 81000, the two isozymes are monomers both in their apoforms and when bound to the enzymatic intermediate biotinyl 5'-AMP, equilibrium sedimentation centrifugation
More
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
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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
Results 1 - 8 of 8