Type | Description |
---|---|
Definition | phenylalanine hydroxylase |
Date | Results | Publications |
---|---|---|
2018-05-05 10:20:00 | results support a model for allostery in PheH in which phenylalanine stabilizes the dimerization of the regulatory domains and exposes the active site for substrate binding and other structural changes needed for activity | 27145334 |
2016-08-20 10:09:00 | The results identify the location of the allosteric site as the interface of the regulatory domain dimer formed in activated PheH. | 26823465 |
2016-08-06 10:33:00 | use of SAXS and X-ray crystallography together to inspect PAH structure provides, to our knowledge, the first complete view of the enzyme in a tetrameric form that was not possible with prior partial crystal structures | 26884182 |
2015-11-07 10:27:00 | allosteric activation of phenylalanine hydroxylase is linked to dimerization of regulatory domains | 26252467 |
2015-02-21 11:12:00 | Data suggest that phenylalanine [concentration-dependent] activation of phenylalanine hydroxylase does not involve the active site; mutating the active-site residue Arg270 to lysine abolishes phenylalanine-dependent enzyme activation. | 25453233 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
Q6AYW2_RAT
UniprotKB:
Q6AYW2
UniParc:
UPI000019B809
EMBL:
BC078881,
CH473960,
AABR07056515,
AABR07056516,
AABR07056517
Ensembl:
ENSRNOG00000004302
KO:
rno:24616
|
Nucleutide sequences |
EMBL-CDS:
EDM17035.1,
AAH78881.1
Gene_ORFName:
rCG_48893
Ensembl_TRS:
ENSRNOT00000005844
|
Protein sequencees |
Ensembl_PRO:
ENSRNOP00000005844
RefSeq:
NP_036751.2,
XP_008763437.1
|
Others |
UniRef100:
UniRef100_Q6AYW2
UniRef90:
UniRef90_P00439
UniRef50:
UniRef50_P00439
UniGene:
Rn.1652
|
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Refseq |
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