KEGG ENZYME: 4.3.1.25

KEGG

ENZYME: 4.3.1.25

Entry

EC 4.3.1.25                 Enzyme

Name

phenylalanine/tyrosine ammonia-lyase;
PTAL;
bifunctional PAL

Class

Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases

Sysname

L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase

Reaction(IUBMB)

(1) L-phenylalanine = trans-cinnamate + NH3 [RN:R00697];
(2) L-tyrosine = trans-p-hydroxycinnamate + NH3 [RN:R00737]

Reaction(KEGG)

R00697 R00737;
(other) R06132

Substrate

L-phenylalanine [CPD:C00079];
L-tyrosine [CPD:C00082]

Product

trans-cinnamate [CPD:C00423];
NH3 [CPD:C00014];
trans-p-hydroxycinnamate [CPD:C00811]

Comment

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), EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency [3]. 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 [4].

History

EC 4.3.1.25 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)

Pathway

Phenylalanine metabolism

Phenylpropanoid biosynthesis

Metabolic pathways

Biosynthesis of secondary metabolites

Orthology

phenylalanine/tyrosine ammonia-lyase

Genes

OSA:

4330034

Os02t0626100-01(Os02g0626100) Os04t0518100-01(Os04g0518100)

OBR:

102717680

OGL:

127764519

BDI:

100839236

ATS:	109753501 109753502 109764465 109782978 109783107 109786255

TDC:	119270978 119279096 119280476 119317181 119320474

123057580 123064291 123064383 123073645 123073646 123099255 123100813 123137534 123144878 542819

TUA:	125547568 125547608

127300268 127307030

LRD:	124658175 124658180 124692572 124692590

SBI:	8054282 8074774

ZMA:

542258

101756300 101766005 101780319

SVS:	117861038 117862866 117864498

120656506 120709319

112882472

Reference

1 [PMID:9008393]

Authors

Rosler J, Krekel F, Amrhein N, Schmid J

Title

Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity.

Journal

Plant Physiol 113:175-9 (1997)
DOI:10.1104/pp.113.1.175

Sequence

[zma:542258]

Reference

2 [PMID:17185227]

Authors

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

Title

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

Journal

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

Reference

3 [PMID:17185228]

Authors

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

Title

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

Journal

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

Reference

4 [PMID:10220322]

Authors

Schwede TF, Retey J, Schulz GE

Title

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

Journal

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

Other DBs

ExplorEnz - The Enzyme Database:

IUBMB Enzyme Nomenclature:

ExPASy - ENZYME nomenclature database:

BRENDA, the Enzyme Database:

DBGET integrated database retrieval system