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The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism†
Cyril Dreyfus,Manuel Larrouy,Florine Cavelier,Jean Martinez,David Pignol,Pascal Arnoux
Chemical Communications Pub Date : 04/12/2011 00:00:00 , DOI:10.1039/C1CC10565E
Abstract

We determined the three-dimensional structure of a complex between an archaeal nicotianamine synthase homologue and a chemically synthesised reaction intermediate. This structure suggests that the enzymes cavity allows both an ordered substrate binding and provides energetic coupling of the reaction intermediate formation and translocation.

Graphical abstract: The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism
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