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2agw

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{{STRUCTURE_2agw| PDB=2agw | SCENE= }}
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'''Crystal structure of tryptamine-reduced aromatic amine dehydrogenase (AADH) from Alcaligenes faecalis in complex with tryptamine'''
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===Crystal structure of tryptamine-reduced aromatic amine dehydrogenase (AADH) from Alcaligenes faecalis in complex with tryptamine===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16614214}}
==About this Structure==
==About this Structure==
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[[Category: Sutcliffe, M J.]]
[[Category: Sutcliffe, M J.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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Revision as of 21:29, 27 July 2008

Image:2agw.png

Template:STRUCTURE 2agw

Crystal structure of tryptamine-reduced aromatic amine dehydrogenase (AADH) from Alcaligenes faecalis in complex with tryptamine

Template:ABSTRACT PUBMED 16614214

About this Structure

Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 00:29:10 2008

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