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Phenylalanine aminomutase (L-beta-phenylalanine forming) (EC 5.4.3.10) (Phenylalanine ammonia-lyase) (EC 4.3.1.24)

 PAM_TAXWC               Reviewed;         687 AA.
Q68G84;
03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
07-JUN-2017, entry version 89.
RecName: Full=Phenylalanine aminomutase (L-beta-phenylalanine forming);
EC=5.4.3.10 {ECO:0000269|PubMed:15878763, ECO:0000269|PubMed:22113970};
AltName: Full=Phenylalanine ammonia-lyase;
EC=4.3.1.24 {ECO:0000250|UniProtKB:Q6GZ04};
Name=pam;
Taxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Cupressales; Taxaceae; Taxus.
NCBI_TaxID=29808;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=15878763; DOI=10.1016/j.abb.2005.04.012;
Steele C.L., Chen Y., Dougherty B.A., Li W., Hofstead S., Lam K.S.,
Xing Z., Chiang S.J.;
"Purification, cloning, and functional expression of phenylalanine
aminomutase: the first committed step in Taxol side-chain
biosynthesis.";
Arch. Biochem. Biophys. 438:1-10(2005).
[2]
X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, MUTAGENESIS OF ASN-231;
GLN-319; TYR-322; ARG-325; ASN-355 AND PHE-371, ACTIVE SITE, AND PTM.
PubMed=22113970; DOI=10.1002/anie.201106372;
Wu B., Szymanski W., Wybenga G.G., Heberling M.M., Bartsch S.,
de Wildeman S., Poelarends G.J., Feringa B.L., Dijkstra B.W.,
Janssen D.B.;
"Mechanism-inspired engineering of phenylalanine aminomutase for
enhanced beta-regioselective asymmetric amination of cinnamates.";
Angew. Chem. Int. Ed. 51:482-486(2012).
[3]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH
TRANS-CINNAMATE, FUNCTION, ACTIVE SITE, PTM, SUBUNIT, AND MUTAGENESIS
OF TYR-80; ASN-231 AND TYR-322.
PubMed=24786474; DOI=10.1021/bi500187a;
Wybenga G.G., Szymanski W., Wu B., Feringa B.L., Janssen D.B.,
Dijkstra B.W.;
"Structural investigations into the stereochemistry and activity of a
phenylalanine-2,3-aminomutase from Taxus chinensis.";
Biochemistry 53:3187-3198(2014).
-!- FUNCTION: Phenylalanine aminomutase that catalyzes the
rearrangement of L-phenylalanine to R-beta-phenylalanine.
Catalyzes the first committed step in the biosynthesis of the side
chain of the alkaloid taxol (paclitaxel), a widely-used compound
with antitumor activity. Has also low phenylalanine ammonia-lyase
activity and can catalyze the amination of trans-cinnamate.
{ECO:0000269|PubMed:15878763, ECO:0000269|PubMed:22113970,
ECO:0000269|PubMed:24786474}.
-!- CATALYTIC ACTIVITY: L-phenylalanine = L-beta-phenylalanine.
{ECO:0000269|PubMed:15878763, ECO:0000269|PubMed:22113970}.
-!- CATALYTIC ACTIVITY: L-phenylalanine = trans-cinnamate + ammonia.
{ECO:0000250|UniProtKB:Q6GZ04}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.1 mM for L-phenylalanine {ECO:0000269|PubMed:15878763,
ECO:0000269|PubMed:22113970};
Vmax=110 umol/min/mg enzyme with L-phenylalanine as substrate
{ECO:0000269|PubMed:15878763, ECO:0000269|PubMed:22113970};
pH dependence:
Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:15878763,
ECO:0000269|PubMed:22113970};
-!- PATHWAY: Alkaloid biosynthesis; taxol biosynthesis.
-!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
trans-cinnamate from L-phenylalanine: step 1/1.
-!- SUBUNIT: Homodimer (PubMed:15878763). Homotetramer, dimer of
dimers (PubMed:24786474). {ECO:0000269|PubMed:15878763,
ECO:0000269|PubMed:24786474}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO),
which is formed autocatalytically by cyclization and dehydration
of residues Ala-Ser-Gly.
-!- BIOTECHNOLOGY: Could be used for the stereoselective biosynthesis
of beta-amino acids via amination of cinnamic acid derivatives.
{ECO:0000269|PubMed:22113970}.
-!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY724735; AAU01182.1; -; mRNA.
PDB; 2YII; X-ray; 2.18 A; A/B/C/D=1-687.
PDB; 4BAA; X-ray; 2.50 A; A/B/C/D=1-687.
PDB; 4BAB; X-ray; 2.56 A; A/B/C/D=1-687.
PDB; 4C5R; X-ray; 2.14 A; A/B/C/D=1-687.
PDB; 4C5S; X-ray; 1.85 A; A/B/C/D=1-79, A/B/C/D=81-687.
PDB; 4C5U; X-ray; 2.19 A; A/B/C/D=1-687.
PDB; 4C6G; X-ray; 2.10 A; A/B/C/D=1-687.
PDB; 4CQ5; X-ray; 1.90 A; A/B/C/D=1-687.
PDB; 4V2Q; X-ray; 1.95 A; A/B=1-687.
PDB; 4V2R; X-ray; 2.20 A; A/B=1-687.
PDBsum; 2YII; -.
PDBsum; 4BAA; -.
PDBsum; 4BAB; -.
PDBsum; 4C5R; -.
PDBsum; 4C5S; -.
PDBsum; 4C5U; -.
PDBsum; 4C6G; -.
PDBsum; 4CQ5; -.
PDBsum; 4V2Q; -.
PDBsum; 4V2R; -.
ProteinModelPortal; Q68G84; -.
SMR; Q68G84; -.
BRENDA; 5.4.3.11; 9720.
UniPathway; UPA00713; UER00725.
UniPathway; UPA00842; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016869; F:intramolecular transferase activity, transferring amino groups; IDA:UniProtKB.
GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IEA:UniProtKB-EC.
GO; GO:0009821; P:alkaloid biosynthetic process; TAS:UniProtKB.
GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
GO; GO:0042617; P:paclitaxel biosynthetic process; TAS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
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.
InterPro; IPR031008; Taxol_Phe_23mut.
Pfam; PF00221; Lyase_aromatic; 1.
SUPFAM; SSF48557; SSF48557; 1.
TIGRFAMs; TIGR01226; phe_am_lyase; 1.
TIGRFAMs; TIGR04473; taxol_Phe_23mut; 1.
PROSITE; PS00488; PAL_HISTIDASE; 1.
1: Evidence at protein level;
3D-structure; Alkaloid metabolism; Cytoplasm;
Direct protein sequencing; Isomerase; Lyase;
Phenylpropanoid metabolism; Taxol biosynthesis.
CHAIN 1 687 Phenylalanine aminomutase (L-beta-
phenylalanine forming).
/FTId=PRO_0000429970.
ACT_SITE 80 80 Proton donor/acceptor.
{ECO:0000269|PubMed:22113970,
ECO:0000269|PubMed:24786474}.
BINDING 231 231 Substrate.
BINDING 319 319 Substrate.
BINDING 325 325 Substrate.
BINDING 355 355 Substrate.
BINDING 458 458 Substrate.
MOD_RES 176 176 2,3-didehydroalanine (Ser).
CROSSLNK 175 177 5-imidazolinone (Ala-Gly).
MUTAGEN 80 80 Y->A,F: Abolishes enzyme activity.
{ECO:0000269|PubMed:24786474}.
MUTAGEN 231 231 N->A: Abolishes the formation of the MIO
cofactor and thereby abolishes enzyme
activity. {ECO:0000269|PubMed:22113970,
ECO:0000269|PubMed:24786474}.
MUTAGEN 231 231 N->X: Abolishes enzyme activity; when
associated with X-355.
{ECO:0000269|PubMed:22113970,
ECO:0000269|PubMed:24786474}.
MUTAGEN 319 319 Q->M: Increases deamination activity with
beta-Phe. Increases beta-regioselectivity
in the amination of cinnamate. Abolishes
enzyme activity; when associated with K-
325. {ECO:0000269|PubMed:22113970}.
MUTAGEN 322 322 Y->A: Abolishes the formation of the MIO
cofactor and thereby abolishes enzyme
activity. {ECO:0000269|PubMed:22113970,
ECO:0000269|PubMed:24786474}.
MUTAGEN 322 322 Y->X: Abolishes enzyme activity; when
associated with X-371.
{ECO:0000269|PubMed:22113970,
ECO:0000269|PubMed:24786474}.
MUTAGEN 325 325 R->K: Increases deamination activity with
beta-Phe. Increases beta-regioselectivity
in the amination of cinnamate. Abolishes
enzyme activity; when associated with M-
319. {ECO:0000269|PubMed:22113970}.
MUTAGEN 355 355 N->X: Abolishes enzyme activity; when
associated with X-231.
{ECO:0000269|PubMed:22113970}.
MUTAGEN 371 371 F->X: Abolishes enzyme activity; when
associated with X-322.
{ECO:0000269|PubMed:22113970}.
HELIX 10 23 {ECO:0000244|PDB:4C5S}.
STRAND 26 33 {ECO:0000244|PDB:4C5S}.
HELIX 37 45 {ECO:0000244|PDB:4C5S}.
STRAND 50 53 {ECO:0000244|PDB:4C5S}.
HELIX 55 74 {ECO:0000244|PDB:4C5S}.
TURN 80 82 {ECO:0000244|PDB:4C5S}.
HELIX 87 89 {ECO:0000244|PDB:4C5S}.
HELIX 97 108 {ECO:0000244|PDB:4C5S}.
HELIX 126 140 {ECO:0000244|PDB:4C5S}.
HELIX 149 160 {ECO:0000244|PDB:4C5S}.
STRAND 163 165 {ECO:0000244|PDB:4C5S}.
STRAND 174 177 {ECO:0000244|PDB:4C5S}.
HELIX 179 189 {ECO:0000244|PDB:4C5S}.
STRAND 196 199 {ECO:0000244|PDB:4C5S}.
TURN 200 202 {ECO:0000244|PDB:4C5S}.
STRAND 203 206 {ECO:0000244|PDB:4C5S}.
HELIX 207 213 {ECO:0000244|PDB:4C5S}.
HELIX 225 230 {ECO:0000244|PDB:4C5S}.
STRAND 231 233 {ECO:0000244|PDB:4C6G}.
HELIX 234 265 {ECO:0000244|PDB:4C5S}.
HELIX 269 272 {ECO:0000244|PDB:4C5S}.
HELIX 274 278 {ECO:0000244|PDB:4C5S}.
HELIX 283 296 {ECO:0000244|PDB:4C5S}.
HELIX 300 310 {ECO:0000244|PDB:4C5S}.
HELIX 313 315 {ECO:0000244|PDB:4C5S}.
HELIX 322 325 {ECO:0000244|PDB:4C5S}.
HELIX 327 349 {ECO:0000244|PDB:4C5S}.
STRAND 355 359 {ECO:0000244|PDB:4C5S}.
HELIX 360 362 {ECO:0000244|PDB:4C5S}.
STRAND 364 366 {ECO:0000244|PDB:4C5S}.
HELIX 374 402 {ECO:0000244|PDB:4C5S}.
HELIX 404 406 {ECO:0000244|PDB:4C5S}.
TURN 407 409 {ECO:0000244|PDB:4C5S}.
HELIX 412 414 {ECO:0000244|PDB:4C5S}.
HELIX 420 422 {ECO:0000244|PDB:4C5S}.
HELIX 427 443 {ECO:0000244|PDB:4C5S}.
HELIX 448 450 {ECO:0000244|PDB:4C5S}.
TURN 455 458 {ECO:0000244|PDB:4C5S}.
STRAND 459 461 {ECO:0000244|PDB:4C5S}.
HELIX 465 517 {ECO:0000244|PDB:4C5S}.
HELIX 522 534 {ECO:0000244|PDB:4C5S}.
HELIX 537 539 {ECO:0000244|PDB:4C5S}.
TURN 540 542 {ECO:0000244|PDB:4C5S}.
HELIX 550 565 {ECO:0000244|PDB:4C5S}.
HELIX 575 603 {ECO:0000244|PDB:4C5S}.
STRAND 613 615 {ECO:0000244|PDB:4V2R}.
HELIX 619 622 {ECO:0000244|PDB:4C5S}.
HELIX 626 633 {ECO:0000244|PDB:4C5S}.
TURN 634 637 {ECO:0000244|PDB:4C5S}.
STRAND 642 644 {ECO:0000244|PDB:4BAA}.
HELIX 649 661 {ECO:0000244|PDB:4C5S}.
TURN 662 665 {ECO:0000244|PDB:4CQ5}.
HELIX 666 672 {ECO:0000244|PDB:4C5S}.
TURN 673 675 {ECO:0000244|PDB:4C5S}.
SEQUENCE 687 AA; 75332 MW; D9BC13C7C689A421 CRC64;
MGFAVESRSH VKDILGLINA FNEVKKITVD GTTPITVAHV AALARRHDVK VALEAEQCRA
RVETCSSWVQ RKAEDGADIY GVTTGFGACS SRRTNRLSEL QESLIRCLLA GVFTKGCAPS
VDELPATATR SAMLLRLNSF TYGCSGIRWE VMEALEKLLN SNVSPKVPLR GSVSASGDLI
PLAYIAGLLI GKPSVIARIG DDVEVPAPEA LSRVGLRPFK LQAKEGLALV NGTSFATAVA
STVMYDANVL LLLVETLCGM FCEVIFGREE FAHPLIHKVK PHPGQIESAE LLEWLLRSSP
FQELSREYYS IDKLKKPKQD RYALRSSPQW LAPLVQTIRD ATTTVETEVN SANDNPIIDH
ANDRALHGAN FQGSAVGFYM DYVRIAVAGL GKLLFAQFTE LMIEYYSNGL PGNLSLGPDL
SVDYGLKGLD IAMAAYSSEL QYLANPVTTH VHSAEQHNQD INSLALISAR KTEEALDILK
LMIASHLTAM CQAVDLRQLE EALVKVVENV VSTLADECGL PNDTKARLLY VAKAVPVYTY
LESPCDPTLP LLLGLKQSCF DTILALHKKD GIETDTLVDR LAEFEKRLSD RLENEMTAVR
VLYEKKGHKT ADNNDALVRI QGSKFLPFYR FVREELDTGV MSARREQTPQ EDVQKVFDAI
ADGRITVPLL HCLQGFLGQP NGCANGV


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