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EC Number
Crystallization (Commentary)
Reference
4.2.2.21
crystal structure identifies additional structurally conserved residues potentially involved in catalysis. A conserved cluster located 12 A from the catalytic tetrad is shown. A His in this cluster is essential for catalysis of dermatane sulfate but not chondroitin sulfate. The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together
692529
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