| Literature DB >> 21820435 |
Takalani Mulaudzi1, Ndiko Ludidi, Oziniel Ruzvidzo, Monique Morse, Nicolette Hendricks, Emmanuel Iwuoha, Chris Gehring.
Abstract
While there is evidence of nitric oxide (NO)-dependent signalling via the second messenger cyclic guanosine 3',5'-monophosphate (cGMP) in plants, guanylate cyclases (GCs), enzymes that catalyse the formation of cGMP from guanosine 5'-triphosphate (GTP) have until recently remained elusive and none of the candidates identified to-date are NO-dependent. Using both a GC and heme-binding domain specific (H-NOX) search motif, we have identified an Arabidopsis flavin monooxygenase (At1g62580) and shown electrochemically that it binds NO, has a higher affinity for NO than for O(2) and that this molecule can generate cGMP from GTP in vitro in an NO-dependent manner.Entities:
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Year: 2011 PMID: 21820435 DOI: 10.1016/j.febslet.2011.07.023
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124