Structural highlights
Function
HOL1_ARATH S-adenosyl-L-methionine-dependent methyltransferase. Involved in glucosinolate metabolism and defense against phytopathogens. Highly reactive to thiocyanate (NCS(-)) derived from myrosinase-mediated hydrolysis of glucosinolates upon tissue damage.[REFERENCE:8][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A product structure of the halomethane producing enzyme in plants (Arabidopsis thaliana) is reported and a model for presentation of chloride/bromide ion to the methyl group of S-adenosyl-L-methionine (SAM) is presented to rationalise nucleophilic halide attack for halomethane production, gaseous natural products that are produced globally.
Halomethane biosynthesis: structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana.,Schmidberger JW, James AB, Edwards R, Naismith JH, O'Hagan D Angew Chem Int Ed Engl. 2010 May 10;49(21):3646-8. doi: 10.1002/anie.201000119. PMID:20376845[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nagatoshi Y, Nakamura T. Arabidopsis HARMLESS TO OZONE LAYER protein methylates a glucosinolate breakdown product and functions in resistance to Pseudomonas syringae pv. maculicola. J Biol Chem. 2009 Jul 17;284(29):19301-9. doi: 10.1074/jbc.M109.001032. Epub 2009, May 6. PMID:19419967 doi:10.1074/jbc.M109.001032
- ↑ Schmidberger JW, James AB, Edwards R, Naismith JH, O'Hagan D. Halomethane biosynthesis: structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana. Angew Chem Int Ed Engl. 2010 May 10;49(21):3646-8. PMID:20376845 doi:10.1002/anie.201000119
