1w27
From Proteopedia
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PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM
Overview
Because of its key role in secondary phenylpropanoid metabolism, Phe, ammonia-lyase is one of the most extensively studied plant enzymes. To, provide a basis for detailed structure-function studies, the enzyme from, parsley (Petroselinum crispum) was crystallized, and the structure was, elucidated at 1.7-A resolution. It contains the unusual electrophilic, 4-methylidene-imidazole-5-one group, which is derived from a tripeptide, segment in two autocatalytic dehydration reactions. The enzyme resembles, His ammonia-lyase from the general His degradation pathway but contains, 207 additional residues, mainly in an N-terminal extension rigidifying a, domain interface and in an inserted alpha-helical domain restricting the, access to the active center. Presumably, Phe ammonia-lyase developed from, His ammonia-lyase when fungi and plants diverged from the other kingdoms., A pathway of the catalyzed reaction is proposed in agreement with, established biochemical data. The inactivation of the enzyme by a, nucleophile is described in detail.
About this Structure
1W27 is a Single protein structure of sequence from Petroselinum crispum with as ligand. Active as Phenylalanine ammonia-lyase, with EC number 4.3.1.5 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase., Ritter H, Schulz GE, Plant Cell. 2004 Dec;16(12):3426-36. Epub 2004 Nov 17. PMID:15548745
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