1pby: Difference between revisions

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[[Image:1pby.gif|left|200px]]
{{Seed}}
[[Image:1pby.png|left|200px]]


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{{STRUCTURE_1pby|  PDB=1pby  |  SCENE=  }}  
{{STRUCTURE_1pby|  PDB=1pby  |  SCENE=  }}  


'''Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution'''
===Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution===




==Overview==
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The 109 kDa quinohemoprotein amine dehydrogenase (QHNDH) from Paracoccus denitrificans contains a novel redox cofactor, cysteine tryptophylquinone (CTQ). This cofactor is derived from a pair of gene-encoded amino acids by post-translational modification and was previously identified and characterized within an 82-residue subunit by chemical methods and crystallographic analysis at 2.05 A resolution. It contains an orthoquinone moiety bound to the indole ring and catalyzes the oxidation of aliphatic and aromatic amines through formation of a Schiff-base intermediate involving one of the quinone O atoms. This paper reports the structural analysis of the complex of QHNDH with the enzyme inhibitor phenylhydrazine determined at 1.70 A resolution. The phenylhydrazone product is attached to the C6 position, identifying the O6 atom of CTQ as the site of Schiff-base formation as postulated by analogy to another amine-oxidizing enzyme, methylamine dehydrogenase. Furthermore, the inner N atom closest to the phenyl ring of phenylhydrazine forms a hydrogen bond to gammaAsp33 in the complex, lending support to the hypothesis that this residue serves as the active-site base for proton abstraction during catalysis.
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{{ABSTRACT_PUBMED_12925784}}


==About this Structure==
==About this Structure==
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[[Category: Amine dehydrogenase]]
[[Category: Amine dehydrogenase]]
[[Category: Quinohemoprotein]]
[[Category: Quinohemoprotein]]
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