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Stringency of the 2-His–1-Asp Active-Site Motif in Prolyl 4-Hydroxylase
[chapter]
2011
Recent Advances in Biochemistry
The non-heme iron(II) dioxygenase family of enzymes contain a common 2-His-1-carboxylate iron-binding motif. These enzymes catalyze a wide variety of oxidative reactions, such as the hydroxylation of aliphatic C-H bonds. Prolyl 4hydroxylase (P4H) is an a-ketoglutarate-dependent iron(II) dioxygenase that catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix. Human P4H residues His412, Asp414, and His483 have been
doi:10.1201/b13131-14
fatcat:jawkx3sjn5b4zefu27zct5b5ca