Description

IPR005922 is a Phenylalanine ammonia-lyase.

<p>The ubiquitous higher plant enzyme phenylalanine ammonia-lyase (PAL; [ec:4.3.1.24]) is a key biosynthetic catalyst in phenylpropanoid assembly. PAL catalyses the non-oxidative deamination of L-phenylalanine to trans-cinnamic acid. PAL contains a catalytic Ala-Ser-Gly triad that is post-translationally cyclised. PAL is structurally similar to the mechanistically related histidine ammonia lyase (HAL; [ec:4.3.1.3]), with PAL having an additional approximately 160 residues extending from the common fold [[cite:PUB00031359]]. Catalysis in PAL may be governed by the dipole moments of seven α-helices associated with the PAL active site. The cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) resides atop the positive poles of three helices, for increasing its electrophillicity. Plant and fungal PAL enzymes contain aa approximately 100-residue long C-terminal multi-helix domain, which might play a role in the rapid response of PAL in the regulation of phenylpropanoid biosynthesis by destabilising the enzyme [[cite:PUB00035855]]. This entry also includes fungal proteins such as Phenylalanine ammonia-lyase CLZ10 which mediates the biosynthesis of squalestatin S1 with potent cholesterol lowering activity by targeting squalene synthase (SS) [[cite:PUB00097889]], and Phenylalanine ammonia-lyase hkm12 involved in the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines [[cite:PUB00097890]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 45

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: