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| [[Image:2o7e.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2o7e| PDB=2o7e | SCENE= }} | | {{STRUCTURE_2o7e| PDB=2o7e | SCENE= }} |
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| '''Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to 2-aminoindan-2-phosphonic acid'''
| | ===Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to 2-aminoindan-2-phosphonic acid=== |
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| ==Overview==
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| Aromatic amino acid ammonia-lyases catalyze the deamination of L-His, L-Phe, and L-Tyr, yielding ammonia plus aryl acids bearing an alpha,beta-unsaturated propenoic acid. We report crystallographic analyses of unliganded Rhodobacter sphaeroides tyrosine ammonia-lyase (RsTAL) and RsTAL bound to p-coumarate and caffeate. His 89 of RsTAL forms a hydrogen bond with the p-hydroxyl moieties of coumarate and caffeate. His 89 is conserved in TALs but replaced in phenylalanine ammonia-lyases (PALs) and histidine ammonia-lyases (HALs). Substitution of His 89 by Phe, a characteristic residue of PALs, yields a mutant with a switch in kinetic preference from L-Tyr to L-Phe. Structures of the H89F mutant in complex with the PAL product, cinnamate, or the PAL-specific inhibitor, 2-aminoindan-2-phosphonate (AIP), support the role of position 89 as a specificity determinant in the family of aromatic amino acid ammonia-lyases and aminomutases responsible for beta-amino acid biosynthesis.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17185228}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17185228 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17185228}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Noel, J P.]] | | [[Category: Noel, J P.]] |
| [[Category: Methylidene imidazolone prosthetic group]] | | [[Category: Methylidene imidazolone prosthetic group]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:24:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:51:10 2008'' |