Type | Description |
---|---|
Definition | purine nucleoside phosphorylase |
Date | Results | Publications |
---|---|---|
2018-09-08 11:54:00 | The study suggests that mass-constrained femtosecond motions at the catalytic site of PNP can improve transition state barrier crossing by more frequent sampling of essential catalytic site contacts. | 29915028 |
2017-12-16 12:31:00 | The PNP rs1049564 T allele is a loss-of-function variant that induces S-phase block and IFN pathway activation in lymphocytes. The S-phase block could be rescued in our in vitro experiments, suggesting the potential for personalized treatment. | 28859258 |
2017-05-27 10:49:00 | Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates. | 27976868 |
2016-09-03 11:30:00 | Data (including data from empirical valence bond/molecular dynamic simulations) suggest that PNP substrate specificity for inosine and guanosine is a direct result of electrostatic preorganization energy along the reaction coordinate. | 26985580 |
2016-02-06 10:20:00 | the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported. | 25625196 |
Type | IDs |
---|---|
Synonymous | NP, PRO1837, PUNP |
Gene |
UniProtKB-ID:
PNPH_HUMAN,
V9HWH6_HUMAN
UniprotKB:
P00491,
V9HWH6
UniParc:
UPI00001FCF7D
EMBL:
X00737,
CH471078,
BC104206,
AY817667,
J02672,
M13952,
M13953,
CR407607,
BC106074,
AK313490,
BC104207,
EU794649,
M13951
Ensembl:
ENSG00000198805
KO:
hsa:4860
|
Nucleutide sequences |
EMBL-CDS:
AAI04208.1,
AAV68044.1,
BAG36272.1,
EAW66458.1,
AAI04207.1,
AAA36460.1,
EAW66459.1,
CAA25320.1,
AAI06075.1,
CAG28535.1,
ACJ13703.1
Ensembl_TRS:
ENST00000361505
|
Protein sequencees |
Ensembl_PRO:
ENSP00000354532
RefSeq:
NP_000261.2
|
Others |
UniRef100:
UniRef100_P00491
UniRef90:
UniRef90_P00491
UniRef50:
UniRef50_P00491
UniGene:
Hs.75514
CCDS:
CCDS9552.1
|
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