Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases

L-phenylalanine ammonia-lyase (trans-cinnamate-forming)

L-phenylalanine = trans-cinnamate + NH3 [RN:R00697]

R00697;
(other) R06132

L-phenylalanine [CPD:C00079]

This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [3]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [9]. The enzyme from some species is highly specific for phenylalanine [7,8].

EC 4.3.1.24 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)

1  [PMID:14458851]

KOUKOL J, CONN EE.

The metabolism of aromatic compounds in higher plans. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare.

J Biol Chem 236:2692-8 (1961)

2

Young, M.R. and Neish, A.C.

Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum.

Phytochemistry 5:1121-1132 (1966)

3  [PMID:17185228]

Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP.

Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.

Chem Biol 13:1327-38 (2006)
DOI:10.1016/j.chembiol.2006.11.011

4  [PMID:15350127]

Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T.

Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis.

Biochemistry 43:11403-16 (2004)
DOI:10.1021/bi049053+

5  [PMID:15548745]

Ritter H, Schulz GE.

Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase.

Plant Cell 16:3426-36 (2004)
DOI:10.1105/tpc.104.025288

[ag:CAA68938]

6  [PMID:17185227]

Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C.

Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.

Chem Biol 13:1317-26 (2006)
DOI:10.1016/j.chembiol.2006.10.008

[npu:Npun_R2068]

7  [PMID:7925471]

Appert C, Logemann E, Hahlbrock K, Schmid J, Amrhein N.

Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.).

Eur J Biochem 225:491-9 (1994)
DOI:10.1111/j.1432-1033.1994.00491.x

[ag:CAA57056 CAA57057]

8  [PMID:15276452]

Cochrane FC, Davin LB, Lewis NG.

The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.

Phytochemistry 65:1557-64 (2004)
DOI:10.1016/j.phytochem.2004.05.006

[ath:AT2G37040 AT3G53260 AT5G04230 AT3G10340]

9  [PMID:10220322]

Schwede TF, Retey J, Schulz GE.

Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.

Biochemistry 38:5355-61 (1999)
DOI:10.1021/bi982929q