2AGX

Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. P212121 form

Summary for 2AGX

• Entry DOI: 10.2210/pdb2agx/pdb
• Related: 2AGL 2AGU 2AGW 2AGY 2AGZ 2AH0 2AH1
• Descriptor: Aromatic amine dehydrogenase, 2-(1H-INDOL-3-YL)ETHANIMINE, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Alcaligenes faecalis; More
• Cellular location: Periplasm: P84887 P84888
• Total number of polymer chains: 4
• Total formula weight: 109382.45

Authors

Masgrau, L.,Roujeinikova, A.,Johannissen, L.O.,Hothi, P.,Basran, J.,Ranaghan, K.E.,Mulholland, A.J.,Sutcliffe, M.J.,Scrutton, N.S.,Leys, D. (deposition date: 2005-07-27, release date: 2006-04-25, Last modification date: 2024-04-03)

Primary citation

Masgrau, L.,Roujeinikova, A.,Johannissen, L.O.,Hothi, P.,Basran, J.,Ranaghan, K.E.,Mulholland, A.J.,Sutcliffe, M.J.,Scrutton, N.S.,Leys, D.
Atomic description of an enzyme reaction dominated by proton tunneling
Science, 312:237-241, 2006

PubMed Abstract: 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.

PubMed: 16614214
DOI: 10.1126/science.1126002

Experimental method

X-RAY DIFFRACTION (2.2 Å)