Structure Histidine decarboxylase

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plp covalently bound hdc @ lysine 305. held in place hydrogen bonds other nearby amino acids. here, active site shown plp bound inhibitory methyl-ester histidine residue, necessary crystallization. generated 4e1o.


histidine decarboxylase group ii pyridoxal-dependent decarboxylase, along aromatic-l-amino-acid decarboxylase, , tyrosine decarboxylase. hdc expressed 74 kda polypeptide not enzymatically functional. after post-translational processing enzyme become active. processing consists of truncating of protein s c-terminal chain, reducing peptide molecular weight 54 kda.


histidine decarboxylase exists homodimer, several amino acids respective opposing chain stabilizing hdc active site. in hdc s resting state, plp covalently bound in schiff base lysine 305, , stabilized several hydrogen bonds nearby amino acids aspartate 273, serine 151 , opposing chain s serine 354. hdc contains several regions sequentially , structurally similar in number of other pyridoxal-dependent decarboxylases. particularly evident in vicinity of active site lysine 305.








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