2agw: Difference between revisions

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[[Image:2agw.~~gif~~|left|200px]]

[[Image:2agw.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16614214}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16614214 is the PubMed ID number.

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==About this Structure==

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[[Category: Sutcliffe, M J.]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 19~~:02:01 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:29:10 2008''

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-[[Image:2agw.gif|left|200px]]
+{{Seed}}
+[[Image:2agw.png|left|200px]]
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 {{STRUCTURE_2agw|  PDB=2agw  |  SCENE=  }}
-'''Crystal structure of tryptamine-reduced aromatic amine dehydrogenase (AADH) from Alcaligenes faecalis in complex with tryptamine'''
+===Crystal structure of tryptamine-reduced aromatic amine dehydrogenase (AADH) from Alcaligenes faecalis in complex with tryptamine===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16614214}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16614214 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16614214}}
 ==About this Structure==
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 [[Category: Sutcliffe, M J.]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:02:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:29:10 2008''