1w27
From Proteopedia
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==Overview== | ==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 ... | + | 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== | ==About this Structure== | ||
| - | 1W27 is a | + | 1W27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Petroselinum_crispum Petroselinum crispum] with DTT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phenylalanine_ammonia-lyase Phenylalanine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.5 4.3.1.5] Structure known Active Site: MI1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W27 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phenylpropanoid metabolism]] | [[Category: phenylpropanoid metabolism]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:48:17 2007'' |
Revision as of 12:42, 5 November 2007
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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 DTT as ligand. Active as Phenylalanine ammonia-lyase, with EC number 4.3.1.5 Structure known Active Site: MI1. 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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