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

Phenylalanine-4-hydroxylase (PAH) (EC 1.14.16.1) (EC 1.14.16.4) (Phe-4-monooxygenase) (Tryptophan 5-hydroxylase) (TRH) (Tryptophan 5-monooxygenase)

 PH4H_DICDI              Reviewed;         441 AA.
Q54XS1;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
25-OCT-2017, entry version 92.
RecName: Full=Phenylalanine-4-hydroxylase;
Short=PAH;
EC=1.14.16.1;
EC=1.14.16.4;
AltName: Full=Phe-4-monooxygenase;
AltName: Full=Tryptophan 5-hydroxylase;
Short=TRH;
AltName: Full=Tryptophan 5-monooxygenase;
Name=pah; ORFNames=DDB_G0278781;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=18835579; DOI=10.1016/j.gene.2008.09.005;
Siltberg-Liberles J., Steen I.H., Svebak R.M., Martinez A.;
"The phylogeny of the aromatic amino acid hydroxylases revisited by
characterizing phenylalanine hydroxylase from Dictyostelium
discoideum.";
Gene 427:86-92(2008).
-!- FUNCTION: Hydroxylates L-tryptophan to 5-hydroxy-L-tryptophan but
does not hydroxylate L-tyrosine to L-DOPA. It uses D-threo-
tetrahydrodictyopterin (DH4), also known as dictyoperin, as a
cofactor. {ECO:0000269|PubMed:18835579}.
-!- CATALYTIC ACTIVITY: L-phenylalanine + tetrahydrobiopterin + O(2) =
L-tyrosine + 4a-hydroxytetrahydrobiopterin.
-!- CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O(2) = 5-
hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion. {ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=620 uM for for L-Phe with BH(4) as cofactor
{ECO:0000269|PubMed:18835579};
KM=90 uM for for L-Phe with DH(4) as cofactor
{ECO:0000269|PubMed:18835579};
KM=49 uM for for BH(4) {ECO:0000269|PubMed:18835579};
KM=39 uM for for DH(4) {ECO:0000269|PubMed:18835579};
Vmax=660 nmol/min/mg enzyme with BH(4) as cofactor (preincubated
with L-Phe) {ECO:0000269|PubMed:18835579};
Vmax=840 nmol/min/mg enzyme with DH(4) as cofactor (preincubated
with L-Phe) {ECO:0000269|PubMed:18835579};
Vmax=1620 nmol/min/mg enzyme with BH(4) as cofactor
(preincubated with BH(4)) {ECO:0000269|PubMed:18835579};
Vmax=1890 nmol/min/mg enzyme with DH(4) as cofactor
(preincubated with DH(4)) {ECO:0000269|PubMed:18835579};
Temperature dependence:
Optimum temperature is 40 degrees Celsius.
{ECO:0000269|PubMed:18835579};
-!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
acetoacetate and fumarate from L-phenylalanine: step 1/6.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18835579}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-8067766, EBI-8067766;
-!- MISCELLANEOUS: This enzyme uses tetrahydrodictyopterin (DH4), a D-
threo isomer of biopterin, and not tetrahydrobiopterin (TH4) for
it's catalytic activity.
-!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
hydroxylase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AAFI02000024; EAL67992.1; -; Genomic_DNA.
RefSeq; XP_641959.1; XM_636867.1.
PDB; 5JK5; X-ray; 2.07 A; A/B=1-415.
PDB; 5JK6; X-ray; 2.07 A; A/B=1-415.
PDB; 5JK8; X-ray; 2.39 A; A/B=1-415.
PDBsum; 5JK5; -.
PDBsum; 5JK6; -.
PDBsum; 5JK8; -.
ProteinModelPortal; Q54XS1; -.
SMR; Q54XS1; -.
MINT; MINT-8392800; -.
STRING; 44689.DDB0231664; -.
PaxDb; Q54XS1; -.
EnsemblProtists; EAL67992; EAL67992; DDB_G0278781.
GeneID; 8621691; -.
KEGG; ddi:DDB_G0278781; -.
dictyBase; DDB_G0278781; pah.
eggNOG; KOG3820; Eukaryota.
eggNOG; COG3186; LUCA.
InParanoid; Q54XS1; -.
KO; K00500; -.
OMA; YEFFVEC; -.
PhylomeDB; Q54XS1; -.
Reactome; R-DDI-209905; Catecholamine biosynthesis.
Reactome; R-DDI-209931; Serotonin and melatonin biosynthesis.
Reactome; R-DDI-71182; Phenylalanine and tyrosine catabolism.
SABIO-RK; Q54XS1; -.
UniPathway; UPA00139; UER00337.
PRO; PR:Q54XS1; -.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IDA:dictyBase.
GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
GO; GO:0034617; F:tetrahydrobiopterin binding; IDA:dictyBase.
GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IEA:UniProtKB-EC.
GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
GO; GO:0006559; P:L-phenylalanine catabolic process; IDA:dictyBase.
GO; GO:0051262; P:protein tetramerization; IDA:dictyBase.
GO; GO:0006571; P:tyrosine biosynthetic process; IDA:dictyBase.
Gene3D; 1.10.800.10; -; 1.
InterPro; IPR002912; ACT_dom.
InterPro; IPR001273; ArAA_hydroxylase.
InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
InterPro; IPR036951; ArAA_hydroxylase_sf.
InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
InterPro; IPR018528; Preph_deHydtase_CS.
InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
PANTHER; PTHR11473; PTHR11473; 1.
Pfam; PF00351; Biopterin_H; 1.
PIRSF; PIRSF000336; TH; 1.
PRINTS; PR00372; FYWHYDRXLASE.
SUPFAM; SSF56534; SSF56534; 1.
PROSITE; PS51671; ACT; 1.
PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Iron; Metal-binding; Monooxygenase;
Oxidoreductase; Phenylalanine catabolism; Reference proteome.
CHAIN 1 441 Phenylalanine-4-hydroxylase.
/FTId=PRO_0000328336.
DOMAIN 23 102 ACT. {ECO:0000255|PROSITE-
ProRule:PRU01007}.
METAL 273 273 Iron. {ECO:0000250}.
METAL 278 278 Iron. {ECO:0000250}.
METAL 318 318 Iron. {ECO:0000250}.
STRAND 17 26 {ECO:0000244|PDB:5JK5}.
HELIX 32 45 {ECO:0000244|PDB:5JK5}.
STRAND 49 56 {ECO:0000244|PDB:5JK5}.
STRAND 63 74 {ECO:0000244|PDB:5JK5}.
HELIX 79 88 {ECO:0000244|PDB:5JK5}.
TURN 89 91 {ECO:0000244|PDB:5JK5}.
STRAND 95 98 {ECO:0000244|PDB:5JK5}.
STRAND 104 107 {ECO:0000244|PDB:5JK5}.
HELIX 113 119 {ECO:0000244|PDB:5JK5}.
STRAND 125 129 {ECO:0000244|PDB:5JK5}.
TURN 135 138 {ECO:0000244|PDB:5JK5}.
HELIX 140 155 {ECO:0000244|PDB:5JK5}.
HELIX 169 183 {ECO:0000244|PDB:5JK5}.
HELIX 186 189 {ECO:0000244|PDB:5JK5}.
HELIX 192 204 {ECO:0000244|PDB:5JK5}.
HELIX 215 226 {ECO:0000244|PDB:5JK5}.
STRAND 229 232 {ECO:0000244|PDB:5JK5}.
STRAND 234 236 {ECO:0000244|PDB:5JK6}.
HELIX 239 246 {ECO:0000244|PDB:5JK5}.
TURN 247 249 {ECO:0000244|PDB:5JK5}.
STRAND 250 253 {ECO:0000244|PDB:5JK5}.
HELIX 271 277 {ECO:0000244|PDB:5JK5}.
HELIX 279 282 {ECO:0000244|PDB:5JK5}.
HELIX 285 298 {ECO:0000244|PDB:5JK5}.
HELIX 303 314 {ECO:0000244|PDB:5JK5}.
TURN 315 319 {ECO:0000244|PDB:5JK5}.
STRAND 321 324 {ECO:0000244|PDB:5JK5}.
STRAND 327 330 {ECO:0000244|PDB:5JK5}.
HELIX 333 336 {ECO:0000244|PDB:5JK5}.
HELIX 339 345 {ECO:0000244|PDB:5JK5}.
STRAND 350 354 {ECO:0000244|PDB:5JK5}.
HELIX 357 360 {ECO:0000244|PDB:5JK5}.
STRAND 367 369 {ECO:0000244|PDB:5JK5}.
STRAND 372 378 {ECO:0000244|PDB:5JK5}.
HELIX 380 393 {ECO:0000244|PDB:5JK5}.
STRAND 397 403 {ECO:0000244|PDB:5JK5}.
TURN 404 407 {ECO:0000244|PDB:5JK5}.
STRAND 408 413 {ECO:0000244|PDB:5JK5}.
SEQUENCE 441 AA; 50415 MW; D02E03F28A873D1C CRC64;
MESNTNSQGQ GIIPQSYHSS IFFSISKGSD KIGGLLEYLE IIKKHNINIT RIESRPSKTE
KKDYDFFLDL EYPTENNKEV EKVIKDLEEK GVKATTLQES SNQTYAPWFP RKISDLDLFA
NKVLEMGSDL TSDHPGASDP VYRERRREIA KIASTYKHGD EIPRIDYTEE EIKTWGVVYN
RLKELFPTNA CHQHAYIFPL LEQNCGYSPD NIPQLQDISN FLQECTGWRI RPVQGLLSAR
DFLNGLAFRV FHATQYIRHP SVPLYTPEPD CCHELLGHVP LLADPDFADF SQEIGLASIG
ASDEDIQLLS TCYWFTVEFG LCKEGDTIRA YGAGILSSTG EMEHFLTDKA KKLPFNPFDA
CNTEYPITTF QPLYYVAESF QKAKEQMRQF ADSFKKPFSI RYNPYTQSIE ILDNKDKLLN
ICNDIRNQSE ILADAISKLK A


Related products :

Catalog number Product name Quantity
EIAAB43551 Homo sapiens,Human,Neuronal tryptophan hydroxylase,NTPH,TPH2,Tryptophan 5-hydroxylase 2,Tryptophan 5-monooxygenase 2
EIAAB43552 Neuronal tryptophan hydroxylase,Ntph,Rat,Rattus norvegicus,Tph2,Tryptophan 5-hydroxylase 2,Tryptophan 5-monooxygenase 2
EIAAB43553 Mouse,Mus musculus,Neuronal tryptophan hydroxylase,Ntph,Tph2,Tryptophan 5-hydroxylase 2,Tryptophan 5-monooxygenase 2
18-003-42486 Tryptophan 5-hydroxylase 2 - EC 1.14.16.4; Tryptophan 5-monooxygenase 2; Neuronal tryptophan hydroxylase Polyclonal 0.05 mg Aff Pur
EIAAB43548 Oryctolagus cuniculus,Rabbit,TPH,TPH1,Tryptophan 5-hydroxylase 1,Tryptophan 5-monooxygenase 1
EIAAB43550 Rat,Rattus norvegicus,Tph,Tph1,Tryptophan 5-hydroxylase 1,Tryptophan 5-monooxygenase 1
EIAAB43547 Mouse,Mus musculus,Tph,Tph1,Tryptophan 5-hydroxylase 1,Tryptophan 5-monooxygenase 1
EIAAB43549 Homo sapiens,Human,TPH,TPH1,TPRH,TRPH,Tryptophan 5-hydroxylase 1,Tryptophan 5-monooxygenase 1
18-662-20082 Tryptophan 5-hydroxylase 1 - EC 1.14.16.4; Tryptophan 5-monooxygenase 1 Polyclonal 0.1 ml
18-662-20083 Tryptophan 5-hydroxylase 1 - EC 1.14.16.4; Tryptophan 5-monooxygenase 1 Polyclonal 0.1 ml
18-662-20021 Tryptophan 5-hydroxylase 1 - EC 1.14.16.4; Tryptophan 5-monooxygenase 1 Polyclonal 0.1 ml
EIAAB43546 Chicken,Gallus gallus,TPH,TPH1,Tryptophan 5-hydroxylase 1,Tryptophan 5-monooxygenase 1
AM05146PU-N Tryptophan Hydroxylase (TRH), Tyrosine Hydroxylase (TYH), Phenylalanine Hydroxylase (PAH) Clone PH8 antibody Isotype IgG Host Mouse 0.5 mg
MD-14-0594 Mouse Anti-Tryptophan Hydroxylase, Tyrosine Hydroxylase and Phenylalanine Hydroxylase 500
AM05146PU-N Tryptophan Hydroxylase (TRH), Tyrosine Hydroxylase (TYH), Phenylalanine Hydroxylase (PAH) 0.5 mg
AM05146PU-N Tryptophan Hydroxylase (TRH), Tyrosine Hydroxylase (TYH), Phenylalanine Hydroxylase (PAH) 0.5 mg
MA1099 Monoclonal Antibodies: Tryptophan hydroxylase; reactive species: Human, rat, rabbit.; Clone: Try-63; Isotype: IgG3; Specificity: Tryptophan hydroxylase 100?g
MA1099 Monoclonal Anti-Tryptophan Hydroxylase, Clone number: Try-63, Ig type: mouse IgG3, Immunogen: Recombinant rabbit tryptophan hydroxylase., Specificity: Human;rat;rabbit. No cross reactivity with other 100μg/vial
LF-MA50099 anti-Tryptophan Hydroxylase (Try-63), Mouse monoclonal to Tryptophan Hydroxylase, Isotype IgG3, Host Mouse 200 ul
AHP1307 RABBIT ANTI RAT TRYPTOPHAN HYDROXYLASE 2 (pSer19), Product Type Polyclonal Antibody, Specificity TRYPTOPHAN HYDROXYLASE 2 , Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal 0.1 ml
SCH-AHP1307 RABBIT ANTI RAT TRYPTOPHAN HYDROXYLASE 2 (pSer19), Product Type Polyclonal Antibody, Specificity TRYPTOPHAN HYDROXYLASE 2 , Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal 0.1 ml
SCH-AHP930 SHEEP ANTI TRYPTOPHAN HYDROXYLASE, Product Type Polyclonal Antibody, Specificity TRYPTOPHAN HYDROXYLASE, Target Species Human, Host Sheep, Format Purified, Isotypes Polyclonal IgG, Applications 0.1 ml
AHP930 SHEEP ANTI TRYPTOPHAN HYDROXYLASE, Product Type Polyclonal Antibody, Specificity TRYPTOPHAN HYDROXYLASE, Target Species Human, Host Sheep, Format Purified, Isotypes Polyclonal IgG, Applications 0.1 ml
SCH-AHP918 RABBIT ANTI TRYPTOPHAN HYDROXYLASE (pSer58), Product Type Polyclonal Antibody, Specificity TRYPTOPHAN HYDROXYLASE , Target Species Rabbit, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, 0.1 ml
AHP918 RABBIT ANTI TRYPTOPHAN HYDROXYLASE (pSer58), Product Type Polyclonal Antibody, Specificity TRYPTOPHAN HYDROXYLASE , Target Species Rabbit, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, 0.1 ml


 

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