1w27: Difference between revisions

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[[Image:1w27.gif|left|200px]]
{{Seed}}
[[Image:1w27.png|left|200px]]


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{{STRUCTURE_1w27|  PDB=1w27  |  SCENE=  }}  
{{STRUCTURE_1w27|  PDB=1w27  |  SCENE=  }}  


'''PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM'''
===PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_15548745}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15548745}}


==About this Structure==
==About this Structure==
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[[Category: Mio]]
[[Category: Mio]]
[[Category: Phenylpropanoid metabolism]]
[[Category: Phenylpropanoid metabolism]]
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Revision as of 13:02, 29 July 2008

File:1w27.png

Template:STRUCTURE 1w27

PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM

Template:ABSTRACT PUBMED 15548745

About this Structure

1W27 is a Single protein structure of sequence from Petroselinum crispum. 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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