2nyn
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(New page: 200px<br /><applet load="2nyn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nyn, resolution 1.90Å" /> '''Crystal structure of...)
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Revision as of 19:02, 29 January 2008
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Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis
Overview
Phenylalanine ammonia lyase (PAL) catalyzes the deamination of, phenylalanine to cinnamate and ammonia. While PALs are common in, terrestrial plants where they catalyze the first committed step in the, formation of phenylpropanoids, only a few prokaryotic PALs have been, identified to date. Here we describe for the first time PALs from, cyanobacteria, in particular, Anabaena variabilis ATCC 29413 and Nostoc, punctiforme ATCC 29133, identified by screening the genome sequences of, these organisms for members of the aromatic amino acid ammonia lyase, family. Both PAL genes associate with secondary metabolite biosynthetic, gene clusters as observed for other eubacterial PAL genes. In comparison, to eukaryotic homologues, the cyanobacterial PALs are 20% smaller in size, but share similar substrate selectivity and kinetic activity toward, L-phenylalanine over L-tyrosine. Structure elucidation by protein X-ray, crystallography confirmed that the two cyanobacterial PALs are similar in, tertiary and quatenary structure to plant and yeast PALs as well as the, mechanistically related histidine ammonia lyases.
About this Structure
2NYN is a Single protein structure of sequence from Anabaena variabilis. Active as Histidine ammonia-lyase, with EC number 4.3.1.3 Full crystallographic information is available from OCA.
Reference
Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization., Moffitt MC, Louie GV, Bowman ME, Pence J, Noel JP, Moore BS, Biochemistry. 2007 Jan 30;46(4):1004-12. PMID:17240984
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