2AGY: Crystal Structure Of The Schiff Base Intermediate In The Reductive Half-Reaction Of Aromatic Amine Dehydrogenase (Aadh) With Tryptamine. Monoclinic Form

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.
PDB ID: 2AGYDownload
MMDB ID: 38544
PDB Deposition Date: 2005/7/27
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.1  Å
Source Organism:
Similar Structures:
Biological Unit for 2AGY: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 2AGY
Label Count Molecule
Proteins (4 molecules)
Aromatic Amine Dehydrogenase
Molecule annotation
Aromatic Amine Dehydrogenase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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