1W27

Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum

Summary for 1W27

• Entry DOI: 10.2210/pdb1w27/pdb
• Descriptor: PHENYLALANINE AMMONIA-LYASE 1, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• Functional Keywords: lyase, phenylpropanoid metabolism, mio
• Biological source: PETROSELINUM CRISPUM (PARSLEY)
• Cellular location: Cytoplasm (Probable): P24481
• Total number of polymer chains: 2
• Total formula weight: 156065.96

Authors

Ritter, H.,Schulz, G.E. (deposition date: 2004-06-29, release date: 2004-11-25, Last modification date: 2023-11-15)

Primary citation

Ritter, H.,Schulz, G.E.
Structural Basis for the Entrance Into the Phenylpropanoid Metabolism Catalyzed by Phenylalanine Ammonia-Lyase
Plant Cell, 16:3426-, 2004

PubMed Abstract: 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.

PubMed: 15548745
DOI: 10.1105/TPC.104.025288

Experimental method

X-RAY DIFFRACTION (1.7 Å)