Structural highlights
Function
O26771_METTH
Publication Abstract from PubMed
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.
The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism.,Dreyfus C, Larrouy M, Cavelier F, Martinez J, Pignol D, Arnoux P Chem Commun (Camb). 2011 May 28;47(20):5825-7. Epub 2011 Apr 12. PMID:21487608[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dreyfus C, Larrouy M, Cavelier F, Martinez J, Pignol D, Arnoux P. The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism. Chem Commun (Camb). 2011 May 28;47(20):5825-7. Epub 2011 Apr 12. PMID:21487608 doi:10.1039/c1cc10565e
