2agx
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Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. P212121 form
OverviewOverview
We present an atomic-level description of the reaction chemistry of an, enzyme-catalyzed reaction dominated by proton tunneling. By solving, structures of reaction intermediates at near-atomic resolution, we have, identified the reaction pathway for tryptamine oxidation by aromatic amine, dehydrogenase. Combining experiment and computer simulation, we show, proton transfer occurs predominantly to oxygen O2 of Asp(128)beta in a, reaction dominated by tunneling over approximately 0.6 angstroms. The role, of long-range coupled motions in promoting tunneling is controversial. We, show that, in this enzyme system, tunneling is promoted by a short-range, motion modulating proton-acceptor distance and no long-range coupled, motion is required.
About this StructureAbout this Structure
2AGX is a Protein complex structure of sequences from Alcaligenes faecalis with TSH as ligand. Active as Aralkylamine dehydrogenase, with EC number 1.4.99.4 Full crystallographic information is available from OCA.
ReferenceReference
Atomic description of an enzyme reaction dominated by proton tunneling., Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D, Science. 2006 Apr 14;312(5771):237-41. PMID:16614214
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