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| {{STRUCTURE_2nyn| PDB=2nyn | SCENE= }} | | {{STRUCTURE_2nyn| PDB=2nyn | SCENE= }} |
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| '''Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis'''
| | ===Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17240984}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17240984 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17240984}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pence, J.]] | | [[Category: Pence, J.]] |
| [[Category: Methylidene imidazolone prosthetic group]] | | [[Category: Methylidene imidazolone prosthetic group]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:05:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:44:20 2008'' |