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Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25) (Bifunctional phenylalanine ammonia-lyase) (Bifunctional PAL)

 PALY_MAIZE              Reviewed;         703 AA.
Q8VXG7;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
05-JUL-2017, entry version 96.
RecName: Full=Phenylalanine/tyrosine ammonia-lyase;
EC=4.3.1.25;
AltName: Full=Bifunctional phenylalanine ammonia-lyase;
Short=Bifunctional PAL;
Name=PAL1;
Zea mays (Maize).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
Zea.
NCBI_TaxID=4577;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9008393; DOI=10.1104/pp.113.1.175;
Roesler J., Krekel F., Amrhein N., Schmid J.;
"Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase
activity.";
Plant Physiol. 113:175-179(1997).
-!- FUNCTION: Catalyzes the non-oxidative deamination of L-
phenylalanine and L-tyrosine to form trans-cinnamic acid and p-
coumaric acid respectively with similar efficiencies. Facilitates
the commitment step in phenylpropanoid pathways that produce
lignins, coumarins and flavonoids. {ECO:0000269|PubMed:9008393}.
-!- CATALYTIC ACTIVITY: L-phenylalanine = trans-cinnamate + ammonia.
{ECO:0000269|PubMed:9008393}.
-!- CATALYTIC ACTIVITY: L-tyrosine = trans-p-hydroxycinnamate +
ammonia. {ECO:0000269|PubMed:9008393}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=658 uM for L-phenylalanine (at pH 7.7)
{ECO:0000269|PubMed:9008393};
KM=270 uM for L-phenylalanine (at pH 8.7)
{ECO:0000269|PubMed:9008393};
KM=41 uM for L-tyrosine (at pH 7.7)
{ECO:0000269|PubMed:9008393};
KM=19 uM for L-tyrosine (at pH 8.7)
{ECO:0000269|PubMed:9008393};
Note=kcat is 10.6 sec(-1) with L-phenylalanine as substrate and
0.92 sec(-1) with L-tyrosine as substrate (at pH 8.7).;
pH dependence:
Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:9008393};
Temperature dependence:
Optimum temperature is 55-60 degrees Celsius.
{ECO:0000269|PubMed:9008393};
-!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
trans-cinnamate from L-phenylalanine: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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EMBL; L77912; AAL40137.1; -; mRNA.
UniGene; Zm.15903; -.
UniGene; Zm.160760; -.
UniGene; Zm.98094; -.
ProteinModelPortal; Q8VXG7; -.
SMR; Q8VXG7; -.
STRING; 4577.GRMZM2G160541_P01; -.
PRIDE; Q8VXG7; -.
BRENDA; 4.3.1.24; 6752.
SABIO-RK; Q8VXG7; -.
UniPathway; UPA00713; UER00725.
Proteomes; UP000007305; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IDA:AgBase.
GO; GO:0052883; F:tyrosine ammonia-lyase activity; IEA:UniProtKB-EC.
GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
GO; GO:0009699; P:phenylpropanoid biosynthetic process; TAS:AgBase.
GO; GO:0016598; P:protein arginylation; IDA:AgBase.
GO; GO:0046898; P:response to cycloheximide; IDA:AgBase.
GO; GO:0009739; P:response to gibberellin; IDA:AgBase.
CDD; cd00332; PAL-HAL; 1.
Gene3D; 1.10.274.20; -; 1.
Gene3D; 1.10.275.10; -; 1.
InterPro; IPR001106; Aromatic_Lyase.
InterPro; IPR024083; Fumarase/histidase_N.
InterPro; IPR008948; L-Aspartase-like.
InterPro; IPR022313; Phe/His_NH3-lyase_AS.
InterPro; IPR005922; Phe_NH3-lyase.
InterPro; IPR023144; Phe_NH3-lyase_shielding_dom.
Pfam; PF00221; Lyase_aromatic; 1.
SUPFAM; SSF48557; SSF48557; 1.
TIGRFAMs; TIGR01226; phe_am_lyase; 1.
PROSITE; PS00488; PAL_HISTIDASE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Lyase; Phenylpropanoid metabolism;
Reference proteome.
CHAIN 1 703 Phenylalanine/tyrosine ammonia-lyase.
/FTId=PRO_0000418895.
ACT_SITE 96 96 Proton donor/acceptor. {ECO:0000250}.
BINDING 341 341 Substrate. {ECO:0000250}.
BINDING 443 443 Substrate. {ECO:0000250}.
BINDING 471 471 Substrate. {ECO:0000250}.
MOD_RES 190 190 2,3-didehydroalanine (Ser).
{ECO:0000255|PROSITE-ProRule:PRU10122}.
CROSSLNK 189 191 5-imidazolinone (Ala-Gly). {ECO:0000250}.
SEQUENCE 703 AA; 74927 MW; 11374FD68516971E CRC64;
MAGNGAIVES DPLNWGAAAA ELAGSHLDEV KRMVAQARQP VVKIEGSTLR VGQVAAVASA
KDASGVAVEL DEEARPRVKA SSEWILDCIA HGGDIYGVTT GFGGTSHRRT KDGPALQVEL
LRHLNAGIFG TGSDGHTLPS EVTRAAMLVR INTLLQGYSG IRFEILEAIT KLLNTGVSPC
LPLRGTITAS GDLVPLSYIA GLITGRPNAQ AVTVDGRKVD AAEAFKIAGI EGGFFKLNPK
EGLAIVNGTS VGSALAATVM YDANVLAVLS EVLSAVFCEV MNGKPEYTDH LTHKLKHHPG
SIEAAAIMEH ILDGSSFMKQ AKKVNELDPL LKPKQDRYAL RTSPQWLGPQ IEVIRAATKS
IEREVNSVND NPVIDVHRGK ALHGGNFQGT PIGVSMDNAR LAIANIGKLM FAQFSELVNE
FYNNGLTSNL AGSRNPSLDY GFKGTEIAMA SYCSELQYLG NPITNHVQSA DEHNQDVNSL
GLVSARKTAE AIDILKLMSS TYIVALCQAV DLRHLEENIK ASVKNTVTQV AKKVLTMNPS
GELSSARFSE KELISAIDRE AVFTYAEDAA SASLPLMQKL RAVLVDHALS SGERGAGALR
VLQDHQVRGG APRGAAPGGG GRPRGVAEGT APVANRIADS RSFPLYRFVR EELGCVFLTG
ERLKSPGEEC NKVFVGISQG KLVDPMLECL KEWDGKPLPI NIK


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