2nyn: Difference between revisions

Revision as of 14:44, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nyn.png

Template:STRUCTURE 2nyn

Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilisCrystal structure of phenylalanine ammonia-lyase from Anabaena variabilis

Template:ABSTRACT PUBMED 17240984

About this StructureAbout this Structure

2NYN is a Single protein structure of sequence from Anabaena variabilis. Full crystallographic information is available from OCA.

ReferenceReference

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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-'''Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis'''
+===Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis===
-==Overview==
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-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.
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 [[Category: Pence, J.]]
 [[Category: Methylidene imidazolone prosthetic group]]
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