1w27

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[[Image:1w27.gif|left|200px]]
[[Image:1w27.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1w27 |SIZE=350|CAPTION= <scene name='initialview01'>1w27</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1w27", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=MI1:Dtt+Binding+Site+For+Chain+B'>MI1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-5-HYDROXY-4-METHYL-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1w27| PDB=1w27 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w27 OCA], [http://www.ebi.ac.uk/pdbsum/1w27 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w27 RCSB]</span>
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}}
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'''PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM'''
'''PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM'''
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[[Category: Ritter, H.]]
[[Category: Ritter, H.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
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[[Category: lyase]]
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[[Category: Lyase]]
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[[Category: mio]]
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[[Category: Mio]]
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[[Category: phenylpropanoid metabolism]]
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[[Category: Phenylpropanoid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:03:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:07 2008''
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Revision as of 10:03, 3 May 2008

Image:1w27.gif

Template:STRUCTURE 1w27

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. 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 Page seeded by OCA on Sat May 3 13:03:03 2008

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