Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 PAM_TAXCA               Reviewed;         698 AA.
Q6GZ04;
03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
31-JAN-2018, entry version 84.
RecName: Full=Phenylalanine aminomutase (L-beta-phenylalanine forming);
EC=5.4.3.10 {ECO:0000269|PubMed:21361343};
AltName: Full=Phenylalanine ammonia-lyase;
EC=4.3.1.24 {ECO:0000269|PubMed:21361343};
Name=pam;
Taxus canadensis (Canadian yew).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Cupressales; Taxaceae; Taxus.
NCBI_TaxID=88032;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15178753; DOI=10.1073/pnas.0403009101;
Jennewein S., Wildung M.R., Chau M., Walker K., Croteau R.;
"Random sequencing of an induced Taxus cell cDNA library for
identification of clones involved in Taxol biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 101:9149-9154(2004).
[2]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH
TRANS-CINNAMATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, PTM, AND
MUTAGENESIS OF TYR-80 AND LEU-104.
PubMed=21361343; DOI=10.1021/bi102067r;
Feng L., Wanninayake U., Strom S., Geiger J., Walker K.D.;
"Mechanistic, mutational, and structural evaluation of a Taxus
phenylalanine aminomutase.";
Biochemistry 50:2919-2930(2011).
-!- 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. Also has low phenylalanine ammonia-lyase
activity. {ECO:0000269|PubMed:21361343}.
-!- CATALYTIC ACTIVITY: L-phenylalanine = L-beta-phenylalanine.
{ECO:0000269|PubMed:21361343}.
-!- CATALYTIC ACTIVITY: L-phenylalanine = trans-cinnamate + ammonia.
{ECO:0000269|PubMed:21361343}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.057 mM for L-phenylalanine;
Note=kcat is 0.053 sec(-1) for L-phenylalanine.;
-!- PATHWAY: Alkaloid biosynthesis; taxol biosynthesis.
-!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
trans-cinnamate from L-phenylalanine: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21361343}.
-!- 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. {ECO:0000250|UniProtKB:Q68G84}.
-!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY582743; AAT47186.1; -; mRNA.
PDB; 3NZ4; X-ray; 2.38 A; A/B=1-698.
PDBsum; 3NZ4; -.
ProteinModelPortal; Q6GZ04; -.
SMR; Q6GZ04; -.
KEGG; ag:AAT47186; -.
KO; K20709; -.
BioCyc; MetaCyc:MONOMER-17466; -.
BRENDA; 5.4.3.10; 6224.
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_sf.
InterPro; IPR031008; Taxol_Phe_23mut.
PANTHER; PTHR10362; PTHR10362; 1.
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; Isomerase; Lyase;
Phenylpropanoid metabolism; Taxol biosynthesis.
CHAIN 1 698 Phenylalanine aminomutase (L-beta-
phenylalanine forming).
/FTId=PRO_0000429969.
ACT_SITE 80 80 Proton donor/acceptor.
BINDING 231 231 Substrate.
BINDING 319 319 Substrate.
BINDING 325 325 Substrate.
BINDING 355 355 Substrate.
BINDING 458 458 Substrate. {ECO:0000250}.
MOD_RES 176 176 2,3-didehydroalanine (Ser).
{ECO:0000250|UniProtKB:Q68G84}.
CROSSLNK 175 177 5-imidazolinone (Ala-Gly).
{ECO:0000250|UniProtKB:Q68G84}.
MUTAGEN 80 80 Y->F: Abolishes enzyme activity.
{ECO:0000269|PubMed:21361343}.
MUTAGEN 104 104 L->A: Decreases enzyme activity.
{ECO:0000269|PubMed:21361343}.
HELIX 10 23 {ECO:0000244|PDB:3NZ4}.
STRAND 26 33 {ECO:0000244|PDB:3NZ4}.
HELIX 37 45 {ECO:0000244|PDB:3NZ4}.
STRAND 50 53 {ECO:0000244|PDB:3NZ4}.
HELIX 55 74 {ECO:0000244|PDB:3NZ4}.
TURN 81 83 {ECO:0000244|PDB:3NZ4}.
HELIX 87 89 {ECO:0000244|PDB:3NZ4}.
HELIX 97 108 {ECO:0000244|PDB:3NZ4}.
STRAND 118 120 {ECO:0000244|PDB:3NZ4}.
HELIX 126 140 {ECO:0000244|PDB:3NZ4}.
HELIX 149 160 {ECO:0000244|PDB:3NZ4}.
STRAND 163 165 {ECO:0000244|PDB:3NZ4}.
HELIX 179 189 {ECO:0000244|PDB:3NZ4}.
STRAND 195 202 {ECO:0000244|PDB:3NZ4}.
STRAND 204 206 {ECO:0000244|PDB:3NZ4}.
HELIX 207 213 {ECO:0000244|PDB:3NZ4}.
HELIX 225 230 {ECO:0000244|PDB:3NZ4}.
HELIX 234 265 {ECO:0000244|PDB:3NZ4}.
HELIX 269 272 {ECO:0000244|PDB:3NZ4}.
HELIX 274 278 {ECO:0000244|PDB:3NZ4}.
HELIX 283 296 {ECO:0000244|PDB:3NZ4}.
HELIX 300 309 {ECO:0000244|PDB:3NZ4}.
HELIX 313 315 {ECO:0000244|PDB:3NZ4}.
HELIX 322 325 {ECO:0000244|PDB:3NZ4}.
HELIX 327 349 {ECO:0000244|PDB:3NZ4}.
STRAND 355 359 {ECO:0000244|PDB:3NZ4}.
HELIX 360 362 {ECO:0000244|PDB:3NZ4}.
STRAND 364 366 {ECO:0000244|PDB:3NZ4}.
HELIX 374 402 {ECO:0000244|PDB:3NZ4}.
HELIX 404 407 {ECO:0000244|PDB:3NZ4}.
HELIX 412 414 {ECO:0000244|PDB:3NZ4}.
HELIX 420 422 {ECO:0000244|PDB:3NZ4}.
HELIX 427 443 {ECO:0000244|PDB:3NZ4}.
HELIX 448 450 {ECO:0000244|PDB:3NZ4}.
TURN 455 458 {ECO:0000244|PDB:3NZ4}.
STRAND 459 461 {ECO:0000244|PDB:3NZ4}.
HELIX 465 517 {ECO:0000244|PDB:3NZ4}.
HELIX 522 534 {ECO:0000244|PDB:3NZ4}.
HELIX 537 539 {ECO:0000244|PDB:3NZ4}.
TURN 540 542 {ECO:0000244|PDB:3NZ4}.
HELIX 550 565 {ECO:0000244|PDB:3NZ4}.
HELIX 574 603 {ECO:0000244|PDB:3NZ4}.
HELIX 620 622 {ECO:0000244|PDB:3NZ4}.
HELIX 626 633 {ECO:0000244|PDB:3NZ4}.
TURN 634 637 {ECO:0000244|PDB:3NZ4}.
STRAND 643 645 {ECO:0000244|PDB:3NZ4}.
HELIX 649 662 {ECO:0000244|PDB:3NZ4}.
HELIX 666 673 {ECO:0000244|PDB:3NZ4}.
SEQUENCE 698 AA; 76532 MW; BE106526C9AA891C CRC64;
MGFAVESRSH VKDILGLINT FNEVKKITVD GTTPITVAHV AALARRHDVK VALEAEQCRA
RVETCSSWVQ RKAEDGADIY GVTTGFGACS SRRTNQLSEL QESLIRCLLA GVFTKGCASS
VDELPATATR SAMLLRLNSF TYGCSGIRWE VMEALEKLLN SNVSPKVPLR GSVSASGDLI
PLAYIAGLLI GKPSVVARIG DDVEVPAPEA LSRVGLRPFK LQAKEGLALV NGTSFATALA
STVMYDANVL LLLVETLCGM FCEVIFGREE FAHPLIHKVK PHPGQIESAE LLEWLLRSSP
FQDLSREYYS IDKLKKPKQD RYALRSSPQW LAPLVQTIRD ATTTVETEVN SANDNPIIDH
ANDRALHGAN FQGSAVGFYM DYVRIAVAGL GKLLFAQFTE LMIEYYSNGL PGNLSLGPDL
SVDYGLKGLD IAMAAYSSEL QYLANPVTTH VHSAEQHNQD INSLALISAR KTEEALDILK
LMIASHLTAM CQAVDLRQLE EALVKVVENV VSTLADECGL PNDTKARLLY VAKAVPVYTY
LESPCDPTLP LLLGLEQSCF GSILALHKKD GIETDTLVDR LAEFEKRLSD RLENEMTAVR
VLYEKKGHKT ADNNDALVRI QGSRFLPFYR FVREELDTGV MSARREQTPQ EDVQKVFDAI
ADGRITVPLL HCLQGFLGQP NGCANGVESF QSVWNKSA


Related products :

Catalog number Product name Quantity
E02P0597 Rat L-Phenylalanine ammonia-lyase ELISA, PAL
E02P0597 Rat L-Phenylalanine ammonia-lyase ELISA, PAL 96 Tests/kit
E02P0597 Rat L-Phenylalanine ammonia-lyase ELISA 96T/kit
E11P0597 Bovine L-Phenylalanine ammonia-lyase ELISA 96T/kit
E14P0597 Sheep L-Phenylalanine ammonia-lyase ELISA, PAL
E03P0597 Mouse L-Phenylalanine ammonia-lyase ELISA, PAL
E12P0597 Chicken L-Phenylalanine ammonia-lyase ELISA 96T/kit
E08P0597 Canine L-Phenylalanine ammonia-lyase ELISA 96T/kit
E14P0597 Sheep L-Phenylalanine ammonia-lyase ELISA 96T/kit
E14P0597 Sheep L-Phenylalanine ammonia-lyase ELISA, PAL 96 Tests/kit
E01P0597 Human L-Phenylalanine ammonia-lyase ELISA, PAL
E12P0597 Chicken L-Phenylalanine ammonia-lyase ELISA, PAL
E07P0597 Porcine L-Phenylalanine ammonia-lyase ELISA 96T/kit
E04P0597 Rabbit L-Phenylalanine ammonia-lyase ELISA, PAL
E08P0597 Canine L-Phenylalanine ammonia-lyase ELISA, PAL
E11P0597 Bovine L-Phenylalanine ammonia-lyase ELISA, PAL
E04P0597 Rabbit L-Phenylalanine ammonia-lyase ELISA 96T/kit
E03P0597 Mouse L-Phenylalanine ammonia-lyase ELISA 96T/kit
E07P0597 Porcine L-Phenylalanine ammonia-lyase ELISA, PAL
E09P0597 Monkey L-Phenylalanine ammonia-lyase ELISA, PAL
E09P0597 Monkey L-Phenylalanine ammonia-lyase ELISA, PAL 96 Tests/kit
E05P0597 Guinea pig L-Phenylalanine ammonia-lyase ELISA, PAL
E08P0597 Canine L-Phenylalanine ammonia-lyase ELISA, PAL 96 Tests/kit
E01P0597 Human L-Phenylalanine ammonia-lyase ELISA, PAL 96 Tests/kit
E07P0597 Porcine L-Phenylalanine ammonia-lyase ELISA, PAL 96 Tests/kit


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur