Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of DPYD_PIG

EC Number:1.3.1.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
dihydropyrimidine dehydrogenase (NADP+)
Q28943
Sus scrofa
1025
111424
Reaction
5,6-dihydrouracil + NADP+ = uracil + NADPH + H+
Other sequences found for EC No. 1.3.1.2

General information:

Sequence
show sequence in fasta format
   0 MAPVLSKDVA DIESILALNP RTQSHAALHS TLAKKLDKKH WKRNPDKNCF HCEKLENNFG
  60 DIKHTTLGER GALREAMRCL KCADAPCQKS CPTHLDIKSF ITSISNKNYY GAAKMIFSDN
 120 PLGLTCGMVC PTSDLCVGGC NLYATEEGSI NIGGLQQFAS EVFKAMNIPQ IRNPCLPSQE
 180 KMPEAYSAKI ALLGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV
 240 VNFEIELMKD LGVKIICGKS LSENEITLNT LKEEGYKAAF IGIGLPEPKT DDIFQGLTQD
 300 QGFYTSKDFL PLVAKSSKAG MCACHSPLPS IRGAVIVLGA GDTAFDCATS ALRCGARRVF
 360 LVFRKGFVNI RAVPEEVELA KEEKCEFLPF LSPRKVIVKG GRIVAVQFVR TEQDETGKWN
 420 EDEDQIVHLK ADVVISAFGS VLRDPKVKEA LSPIKFNRWD LPEVDPETMQ TSEPWVFAGG
 480 DIVGMANTTV ESVNDGKQAS WYIHKYIQAQ YGASVSAKPE LPLFYTPVDL VDISVEMAGL
 540 KFINPFGLAS AAPTTSSSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI VRGTTSGPMY
 600 GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW MELSRKAEAS
 660 GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVQIPFFAKL TPNVTDIVSI
 720 ARAAKEGGAD GVTATNTVSG LMGLKADGTP WPAVGAGKRT TYGGVSGTAI RPIALRAVTT
 780 IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAVQ NQDFTVIQDY CTGLKALLYL
 840 KSIEELQGWD GQSPGTESHQ KGKPVPRIAE LMGKKLPNFG PYLEQRKKII AEEKMRLKEQ
 900 NAAFPPLERK PFIPKKPIPA IKDVIGKALQ YLGTFGELSN IEQVVAVIDE EMCINCGKCY
 960 MTCNDSGYQA IQFDPETHLP TVTDTCTGCT LCLSVCPIID CIRMVSRTTP YEPKRGLPLA
1020 VNPVC
Download this sequence
in fasta format
Download all sequences for 1.3.1.2
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1051757
Yokota H.,Fernandez-Salguero P.,Furuya H.,Lin K.,McBride O.W.,Podschun B.,Schnackerz K.D.,Gonzalez F.J.
cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria.
J. Biol. Chem.
269
23192-23196
1994
1051758
Rosenbaum K.,Jahnke K.,Curti B.,Hagen W.R.,Schnackerz K.D.,Vanoni M.A.
Porcine recombinant dihydropyrimidine dehydrogenase: comparison of the spectroscopic and catalytic properties of the wild-type and C671A mutant enzymes.
Biochemistry
37
17598-17609
1998
1051759
Lohkamp B.,Voevodskaya N.,Lindqvist Y.,Dobritzsch D.
Insights into the mechanism of dihydropyrimidine dehydrogenase from site-directed mutagenesis targeting the active site loop and redox cofactor coordination.
Biochim. Biophys. Acta
1804
2198-2206
2010
1051760
Dobritzsch D.,Schneider G.,Schnackerz K.D.,Lindqvist Y.
Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil.
EMBO J.
20
650-660
2001
1051761
Dobritzsch D.,Ricagno S.,Schneider G.,Schnackerz K.D.,Lindqvist Y.
Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer.
J. Biol. Chem.
277
13155-13166
2002