1w27
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Because of its key role in secondary phenylpropanoid metabolism, Phe | + | 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ritter, H.]] | [[Category: Ritter, H.]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: DTT]] | [[Category: DTT]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
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[[Category: phenylpropanoid metabolism]] | [[Category: phenylpropanoid metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:39 2008'' |
Revision as of 13:39, 21 February 2008
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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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